Campbell Biology Ch4+5
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Questions and Answers

What is the significance of carbon's ability to form four bonds in organic chemistry?

Carbon's ability to form four bonds allows for a vast diversity of organic compounds, enabling the complexity of life.

How did Harold Urey contribute to our understanding of the origin of life?

Harold Urey concluded that abiotic synthesis of organic compounds could occur, suggesting a possible pathway for the origin of life.

Describe the shape of a carbon atom when it is single-bonded to four other atoms.

A carbon atom bonded to four atoms has a tetrahedral shape, forming a pyramid structure.

Explain the significance of hydrocarbons in living organisms and their energy storage capabilities.

<p>Hydrocarbons, though not abundant in living organisms, store high amounts of energy due to their numerous nonpolar bonds.</p> Signup and view all the answers

What distinguishes structural isomers from cis-trans isomers?

<p>Structural isomers differ in the covalent arrangement of atoms, while cis-trans isomers differ in the spatial arrangement around a double bond.</p> Signup and view all the answers

How does the number of isomers change with the size of carbon skeletons?

<p>The number of isomers increases dramatically with larger carbon skeletons, with hundreds or thousands of variants possible.</p> Signup and view all the answers

Why is carbon dioxide not typically considered an organic compound despite containing carbon?

<p>Carbon dioxide is often excluded from the definition of organic compounds since it does not contain hydrogen and lacks traditional carbon bonding.</p> Signup and view all the answers

Define carbon skeletons and their importance in organic chemistry.

<p>Carbon skeletons are chains of carbon atoms that form the backbone of organic molecules, providing structure and functional versatility.</p> Signup and view all the answers

What type of isomerism occurs due to restricted rotation around double bonds?

<p>Cis-trans isomerism occurs because double bonds restrict rotation, affecting the spatial arrangement of atoms.</p> Signup and view all the answers

What are the implications of carbon's chemical versatility in the context of life's diversity?

<p>Carbon's chemical versatility allows for the formation of a wide variety of complex molecules, which is fundamental to the diversity of life.</p> Signup and view all the answers

What role do methyl groups play in biological molecules?

<p>Methyl groups serve as tags on biological molecules and are unresponsive to chemical reactions due to being nonpolar.</p> Signup and view all the answers

How does ATP differ from ADP in terms of its phosphate groups?

<p>ATP consists of three phosphate groups, while ADP has only two phosphate groups after one is split off.</p> Signup and view all the answers

What is the main consequence of hydrolysis in biological processes?

<p>Hydrolysis disassembles polymers into monomers, requiring the input of water molecules.</p> Signup and view all the answers

What are functional groups in the context of molecular biology?

<p>Functional groups are groups of chemicals directly involved in chemical reactions of a molecule, responsible for its characteristics.</p> Signup and view all the answers

Why are six out of the seven chemical groups considered hydrophilic?

<p>All except sulfhydryl groups are hydrophilic, which means they increase the solubility of organic compounds in water.</p> Signup and view all the answers

What is the importance of polymerization in biological systems?

<p>Polymerization is the process of creating polymers, which are essential for forming macromolecules like proteins and nucleic acids.</p> Signup and view all the answers

How do enzymes facilitate biological reactions?

<p>Enzymes speed up chemical reactions by lowering the activation energy needed for those reactions to occur.</p> Signup and view all the answers

What differentiates monomers from polymers?

<p>Monomers are single, repeating units, while polymers are long chains made from multiple monomers linked together.</p> Signup and view all the answers

What is a dehydration reaction and its significance?

<p>A dehydration reaction connects monomers by removing a small molecule, typically water, thereby forming polymers.</p> Signup and view all the answers

How do differences in macromolecule composition help distinguish genetic relationships?

<p>Differences in macromolecule diversity, particularly in DNA and proteins, can indicate the genetic distance between organisms.</p> Signup and view all the answers

What does the structure of estradiol and testosterone reveal about their functions?

<p>Both hormones are structurally similar but differ by the chemical groups attached, which determines their specific roles in sexual characteristics.</p> Signup and view all the answers

What happens during a condensation reaction?

<p>A condensation reaction connects monomers, releasing a small molecule such as water as a byproduct.</p> Signup and view all the answers

Why is ATP described as having potential energy?

<p>ATP does not store energy in a static form; rather, it has the potential to release energy when one phosphate group is hydrolyzed.</p> Signup and view all the answers

What role does ribose play in the structure of ATP?

<p>Ribose is the sugar component of ATP that connects the adenosine to the three phosphate groups.</p> Signup and view all the answers

What is the main structural difference between saturated and unsaturated fats?

<p>Saturated fats have no double bonds between carbon atoms, while unsaturated fats contain one or more double bonds.</p> Signup and view all the answers

What role do adipose cells play in the human body?

<p>Adipose cells store long-term food reserves, cushion vital organs, and provide insulation.</p> Signup and view all the answers

How does hydrogenation affect vegetable oils?

<p>Hydrogenation converts unsaturated fats into saturated fats by adding hydrogen, which can solidify the oil.</p> Signup and view all the answers

What is a phospholipid and its importance in cell membranes?

<p>A phospholipid is a molecule with two fatty acids and a phosphate group that forms a bilayer, crucial for cell membrane structure.</p> Signup and view all the answers

What is cholesterol’s function in animal cells?

<p>Cholesterol contributes to the fluidity of cell membranes and is a precursor for steroid hormones.</p> Signup and view all the answers

Describe the process and consequence of the formation of trans fats.

<p>Trans fats form during the hydrogenation of unsaturated fats, resulting in unique double bond structures that contribute to heart disease.</p> Signup and view all the answers

How do the energy storage capabilities of fats compare to polysaccharides?

<p>Fats can store twice as much energy per gram compared to polysaccharides like starch.</p> Signup and view all the answers

What characteristic of lipid molecules makes them predominantly hydrophobic?

<p>Lipid molecules are mainly hydrophobic due to their nonpolar C-H bonds and minimal polar components.</p> Signup and view all the answers

Why do unsaturated fats have a 'bent' structure?

<p>Unsaturated fats have double bonds that cause kinks in their hydrocarbon chains, preventing tight packing.</p> Signup and view all the answers

What are the health implications of a diet high in saturated fats?

<p>A diet high in saturated fats can lead to cardiovascular diseases like atherosclerosis.</p> Signup and view all the answers

What is the significance of the ester linkage in fat molecules?

<p>Ester linkages are formed when fatty acids bond with glycerol during fat synthesis, essential for fat structure.</p> Signup and view all the answers

Describe the difference between 'cis' and 'trans' double bonds in unsaturated fats.

<p>'Cis' double bonds cause bends in the fatty acid chain, while 'trans' double bonds do not, leading to straighter structures.</p> Signup and view all the answers

In what way do cholesterol levels affect blood vessel health?

<p>High cholesterol levels can lead to plaque formation in blood vessels, increasing the risk of atherosclerosis.</p> Signup and view all the answers

What are triglycerides, and how are they formed?

<p>Triglycerides are fats formed from one glycerol molecule and three fatty acids linked by ester linkages.</p> Signup and view all the answers

What role do hydrogen bonds play in the formation of the 𝛼 helix structure of proteins?

<p>Hydrogen bonds form between every fourth amino acid, stabilizing the helical shape of the protein.</p> Signup and view all the answers

Describe the characteristics of the 𝝱 pleated sheet structure in proteins.

<p>The 𝝱 pleated sheet comprises two or more polypeptide segments lying side by side, connected by hydrogen bonds.</p> Signup and view all the answers

What distinguishes tertiary structure from secondary structure in polypeptides?

<p>Tertiary structure refers to the overall three-dimensional shape stabilized by side chain interactions, while secondary structure involves interactions between backbone constituents.</p> Signup and view all the answers

How do hydrophobic interactions influence protein folding?

<p>Hydrophobic interactions cause nonpolar amino acids to cluster at the protein core, minimizing their contact with water.</p> Signup and view all the answers

Explain the function of disulfide bridges in proteins.

<p>Disulfide bridges form between cysteine side chains, stabilizing the protein's structure by linking different parts of the polypeptide chain.</p> Signup and view all the answers

What is quaternary structure in proteins and provide an example?

<p>Quaternary structure involves the assembly of two or more polypeptide chains into a functional protein, such as hemoglobin.</p> Signup and view all the answers

How does sickle cell disease arise from the primary structure of hemoglobin?

<p>Sickle cell disease results from a substitution of valine for glutamic acid at the sixth amino acid in hemoglobin's primary structure.</p> Signup and view all the answers

What factors contribute to the folding of polypeptide chains within cells?

<p>Folding is influenced by the crowded cellular environment and is aided by other proteins that assist in the process.</p> Signup and view all the answers

What is the main difference between Cis and Trans isomers?

<p>Cis isomers have substituents on the same side of a double bond, while trans isomers have them on opposite sides.</p> Signup and view all the answers

Why are enantiomers significant in pharmaceuticals?

<p>One enantiomer often exhibits a different level of effectiveness or activity in biological systems compared to its counterpart.</p> Signup and view all the answers

What defines an asymmetric carbon atom?

<p>An asymmetric carbon atom is one that is bonded to four different atoms or groups.</p> Signup and view all the answers

How do structural isomers differ from one another?

<p>Structural isomers vary in the covalent arrangement of their atoms, which can include differences in carbon skeleton shape and the position of double bonds.</p> Signup and view all the answers

What is the effect of double bonds on the rotation of atoms in a molecule?

<p>Double bonds restrict the free rotation of atoms, whereas single bonds allow for rotation.</p> Signup and view all the answers

Explain why carbon compounds can form large and complex molecules.

<p>Carbon has four valence electrons, allowing it to form stable covalent bonds with many different elements and create extensive chains or rings.</p> Signup and view all the answers

What are hydrocarbons and where are they primarily found?

<p>Hydrocarbons are organic compounds consisting exclusively of carbon and hydrogen atoms, primarily found in fossil fuels like petroleum.</p> Signup and view all the answers

How does the presence of functional groups influence the characteristics of a molecule?

<p>Functional groups are responsible for the chemical reactions and properties of a molecule, determining its reactivity and interaction with other substances.</p> Signup and view all the answers

Identify the unique property of enantiomers.

<p>Enantiomers are mirror images of each other and cannot be superimposed, much like left and right hands.</p> Signup and view all the answers

What role does carbon dioxide play in plant life?

<p>Carbon dioxide is essential for photosynthesis, as plants convert it into glucose and oxygen.</p> Signup and view all the answers

What are trans fats and how are they related to isomerism?

<p>Trans fats are a type of unsaturated fat where the hydrogen atoms are on opposite sides of a double bond, leading to different health impacts compared to cis fats.</p> Signup and view all the answers

Why is it important that carbon has four free slots in its valence shell?

<p>These four free slots enable carbon to form four stable covalent bonds, allowing for diverse molecular structures.</p> Signup and view all the answers

What implications do isomers have in biological reactions?

<p>Different isomers may have drastically different effects in biological reactions, sometimes leading to significant variations in organism responses.</p> Signup and view all the answers

Describe the relationship between the structure and function of estradiol and testosterone.

<p>Estradiol and testosterone have similar structures but differ in their attached chemical groups, which determine their distinct roles in sexual characteristics.</p> Signup and view all the answers

Why do animals rely more on fats for energy storage compared to plants?

<p>Animals expend more energy than plants, so they store energy in fats rather than starch.</p> Signup and view all the answers

What primary functions do adipose cells serve in mammals?

<p>Adipose cells store long-term food reserves and cushion vital organs while also providing insulation.</p> Signup and view all the answers

How do phospholipids behave in an aqueous environment?

<p>Phospholipids form a bilayer where hydrophilic heads face outward and hydrophobic tails face inward.</p> Signup and view all the answers

Describe the structure of steroids and their function in living organisms.

<p>Steroids consist of a carbon skeleton with four fused rings and serve important roles, such as being components of cell membranes and precursors for hormones.</p> Signup and view all the answers

What role do enzymes play in biological systems?

<p>Enzymes speed up chemical reactions and regulate metabolism by acting as catalysts.</p> Signup and view all the answers

What is a polypeptide and how is it formed?

<p>A polypeptide is a polymer of amino acids formed by peptide bonds through dehydration reactions.</p> Signup and view all the answers

Explain the significance of the 'R' group in amino acids.

<p>The 'R' group determines the properties of each amino acid, influencing hydrophobicity or charge.</p> Signup and view all the answers

What distinguishes primary structure from secondary structure in proteins?

<p>Primary structure is the linear sequence of amino acids, while secondary structure involves coiling and folding stabilized by hydrogen bonds.</p> Signup and view all the answers

What is the difference between globular and fibrous proteins?

<p>Globular proteins are spherical and often function as enzymes, while fibrous proteins are long and provide structural support.</p> Signup and view all the answers

How does the sequence of amino acids influence protein structure?

<p>The amino acid sequence dictates how the polypeptide will fold and arrange itself in three-dimensional space.</p> Signup and view all the answers

What is a peptide bond and how is it formed?

<p>A peptide bond is a covalent bond formed between the amino group of one amino acid and the carboxyl group of another through a dehydration reaction.</p> Signup and view all the answers

Why are high cholesterol levels concerning for health?

<p>High cholesterol levels can lead to atherosclerosis, which increases the risk of heart disease.</p> Signup and view all the answers

What determines a protein's ability to interact with other molecules?

<p>A protein's structure, including its shape and charge distribution, dictates its binding capabilities.</p> Signup and view all the answers

Describe the four levels of protein structure.

<p>Proteins have primary (amino acid sequence), secondary (coils and folds), tertiary (3D shape), and quaternary (multiple polypeptides) structures.</p> Signup and view all the answers

What type of bonding primarily stabilizes the secondary structure of proteins?

<p>Hydrogen bonds primarily stabilize the secondary structure of proteins.</p> Signup and view all the answers

What are carbohydrates primarily composed of?

<p>Carbohydrates are primarily composed of carbon, hydrogen, and oxygen.</p> Signup and view all the answers

How do hydrophobic interactions contribute to protein folding?

<p>Hydrophobic interactions cause nonpolar amino acids to cluster at the core of the protein, away from water.</p> Signup and view all the answers

What stabilizes the tertiary structure of a protein?

<p>The tertiary structure is stabilized by interactions between the side chains and amino acid groups, including hydrogen and ionic bonds.</p> Signup and view all the answers

What is the primary function of glucose in cellular respiration?

<p>Glucose serves as a key energy source that is broken down to release energy for cellular activities.</p> Signup and view all the answers

How does the structure of starch differ from that of cellulose?

<p>Starch consists of glucose monomers with 1-4 glycosidic linkages in the same orientation, while cellulose has alternating orientations of its hydroxyl groups.</p> Signup and view all the answers

What characterizes quaternary structures in proteins?

<p>Quaternary structures are characterized by the association of two or more polypeptide chains that form a functional protein.</p> Signup and view all the answers

What distinguishes monosaccharides like glucose and fructose from one another?

<p>Glucose and fructose are structural isomers, differing in their arrangement of atoms despite having the same chemical formula.</p> Signup and view all the answers

What is the primary structural difference between α-helices and β-pleated sheets?

<p>α-helices are coiled structures stabilized by hydrogen bonds between every fourth amino acid, whereas β-pleated sheets consist of segments lying side by side connected by hydrogen bonds.</p> Signup and view all the answers

Define disaccharides and provide an example.

<p>Disaccharides are carbohydrates composed of two monosaccharides linked by a covalent bond; an example is lactose.</p> Signup and view all the answers

What causes sickle cell disease at a molecular level?

<p>Sickle cell disease is caused by a substitution of valine for glutamic acid at the sixth position of the primary structure of hemoglobin.</p> Signup and view all the answers

What is a glycosidic linkage?

<p>A glycosidic linkage is a covalent bond formed between two monosaccharides through a dehydration reaction.</p> Signup and view all the answers

Describe the role of Van der Waals interactions in protein structure.

<p>Van der Waals interactions help hold nonpolar amino acids together when they cluster in the protein's core.</p> Signup and view all the answers

How does the crowded environment of the cell affect protein folding?

<p>The crowded cellular environment aids in protein folding by promoting interactions between polypeptide chains and other proteins.</p> Signup and view all the answers

Explain why certain polysaccharides, like cellulose, are indigestible by most organisms.

<p>Cellulose is indigestible because the enzymes that hydrolyze starch cannot break the unique glycosidic linkages in cellulose.</p> Signup and view all the answers

What is the role of chitin in biological organisms?

<p>Chitin serves as a structural polysaccharide, providing strength and support in the exoskeletons of arthropods.</p> Signup and view all the answers

How do the properties of saturated fats differ from those of unsaturated fats?

<p>Saturated fats contain no double bonds between carbon atoms, making them solid at room temperature, while unsaturated fats have one or more double bonds and are typically liquid.</p> Signup and view all the answers

What is the significance of the carbon skeleton sizes in sugars?

<p>The size of the carbon skeleton in sugars ranges from 3 to 7 carbons, influencing their classification and functional properties.</p> Signup and view all the answers

Describe how plants utilize sucrose.

<p>Plants transport carbohydrates primarily in the form of sucrose, which consists of glucose and fructose bonded together.</p> Signup and view all the answers

What role do pentoses and hexoses play in forming ring structures?

<p>Pentoses and hexoses tend to form ring structures because this conformation is the most stable for these sugars.</p> Signup and view all the answers

Identify the structural characteristics of glycogen.

<p>Glycogen is a highly branched polysaccharide composed of glucose and functions primarily as an energy storage molecule in animals.</p> Signup and view all the answers

What is meant by the term 'hydrophobic' in relation to fats?

<p>Fats are termed hydrophobic because they do not mix well with water due to their nonpolar nature.</p> Signup and view all the answers

What is denaturation and what environmental factors can cause it?

<p>Denaturation is the process where proteins lose their shape and biological activity due to changes in pH, temperature, or salt concentration.</p> Signup and view all the answers

How does the environment affect the folding of polypeptide chains?

<p>The polypeptide chains fold based on the properties of the surrounding environment, such as solvent polarity, which influences the orientation of hydrophobic and hydrophilic regions.</p> Signup and view all the answers

What role do weak chemical bonds play in protein folding?

<p>Weak chemical bonds, such as hydrogen bonds and ionic bonds, are crucial for stabilizing the various shapes proteins adopt during folding.</p> Signup and view all the answers

Why can certain proteins renature after denaturation, while others cannot?

<p>Some proteins can renature when the denaturing agent is removed if their primary structure remains intact, but others, like cooked egg proteins, cannot.</p> Signup and view all the answers

What is X-ray crystallography used for in protein studies?

<p>X-ray crystallography is used to determine the three-dimensional structure of proteins by analyzing how X-rays diffract through crystallized molecules.</p> Signup and view all the answers

What are intrinsically disordered proteins and why are they significant?

<p>Intrinsically disordered proteins lack a fixed three-dimensional structure until they interact with other molecules, which is critical for their flexibility and functionality.</p> Signup and view all the answers

Describe the relationship between enzyme functionality and protein structure.

<p>Enzymes rely on their specific three-dimensional structure to interact with substrates, facilitating chemical reactions efficiently.</p> Signup and view all the answers

What differentiates a polypeptide from a functional protein?

<p>A polypeptide is a chain of amino acids, whereas a functional protein is one or more polypeptides folded into a specific three-dimensional shape.</p> Signup and view all the answers

How do primary, secondary, tertiary, and quaternary structures contribute to protein function?

<p>Each structure level contributes to the overall shape and stability of the protein, which dictates its ability to perform specific biological functions.</p> Signup and view all the answers

What occurs during the formation of a peptide bond?

<p>A peptide bond forms when the carboxyl group of one amino acid reacts with the amino group of another, releasing a water molecule in a dehydration reaction.</p> Signup and view all the answers

What kind of diseases are associated with misfolded proteins?

<p>Diseases such as cystic fibrosis, Alzheimer's, Parkinson's, and mad cow disease are linked to the accumulation of misfolded proteins.</p> Signup and view all the answers

What type of bonds stabilize secondary protein structures?

<p>Secondary protein structures are stabilized primarily by hydrogen bonds between the backbone atoms of the polypeptide.</p> Signup and view all the answers

Describe the role of catalysts in biological systems.

<p>Catalysts, primarily enzymes, accelerate chemical reactions in biological systems, making them essential for metabolism.</p> Signup and view all the answers

What is denaturation in proteins and what can cause it?

<p>Denaturation refers to the process where proteins lose their shape and become biologically inactive due to alterations in environmental factors like pH, salt concentration, or temperature.</p> Signup and view all the answers

Why can high temperatures be fatal due to denaturation?

<p>High temperatures can lead to denaturation of proteins, causing them to lose their functional shape, which can disrupt critical biological processes.</p> Signup and view all the answers

Describe the primary structure of proteins and its significance.

<p>The primary structure of proteins is defined by the specific sequence of amino acids in a polypeptide chain, which ultimately determines the protein's three-dimensional shape and function.</p> Signup and view all the answers

What role do ribosomes play in protein synthesis?

<p>Ribosomes facilitate the translation of mRNA into polypeptides, which are then folded into functional proteins.</p> Signup and view all the answers

How do purines and pyrimidines differ structurally?

<p>Purines consist of a six-membered ring fused to a five-membered ring, while pyrimidines are composed of a single six-membered ring.</p> Signup and view all the answers

What is the significance of the sugar-phosphate backbone in nucleic acids?

<p>The sugar-phosphate backbone is essential for maintaining the structural stability of nucleic acids and provides directionality to the polynucleotide chain.</p> Signup and view all the answers

What is an antiparallel arrangement in DNA?

<p>Antiparallel arrangement refers to the opposite orientation of the two strands of DNA, where one strand runs 5’ to 3’ while the other runs 3’ to 5’.</p> Signup and view all the answers

Explain the concept of gene expression.

<p>Gene expression is the process through which genetic information in DNA is transcribed into mRNA and translated into proteins, controlling various cellular functions.</p> Signup and view all the answers

What technique is primarily used to determine the 3-D structure of proteins?

<p>X-ray crystallography is the technique used to determine the three-dimensional structure of proteins by analyzing the diffraction of X-rays through crystallized molecules.</p> Signup and view all the answers

How do environmental conditions lead to the misfolding of proteins?

<p>Environmental changes, such as temperature and chemical concentration alterations, can disrupt the delicate interactions that stabilize protein folding, leading to misfolding.</p> Signup and view all the answers

What distinguishes RNA from DNA in terms of structure?

<p>RNA is typically single-stranded and contains ribose sugar, while DNA is double-stranded and contains deoxyribose sugar.</p> Signup and view all the answers

What is the function of phosphodiester linkages in nucleic acids?

<p>Phosphodiester linkages bond nucleotides together in a polynucleotide strand, forming the backbone of nucleic acids through covalent bonds between the sugar of one nucleotide and the phosphate of another.</p> Signup and view all the answers

Describe the process of nucleotide polymerization.

<p>Nucleotide polymerization involves the linkage of nucleotides into polynucleotides through the loss of phosphate groups, forming nucleotide sequences encoded by genetic information.</p> Signup and view all the answers

How do base pairs in DNA contribute to its stability?

<p>Base pairs in DNA contribute to stability through hydrogen bonds between complementary bases (A-T and G-C), which help hold the two DNA strands together.</p> Signup and view all the answers

Flashcards

Organic Chemistry

The study of substances containing carbon.

Abiotic Synthesis

Formation of organic compounds from non-living sources.

Carbon's Bonding

Carbon can form four covalent bonds with other atoms.

Carbon Skeleton

A chain of carbon atoms that forms the backbone of many organic molecules.

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Hydrocarbon

Organic compounds made only of carbon and hydrogen atoms.

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Isomers

Molecules with the same chemical formula but different structures and properties.

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Structural Isomer

Isomers that differ in the arrangement of their atoms.

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Cis-Trans Isomer

Isomers where the atoms differ in their position around a double bond.

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Tetrahedral Shape

The three-dimensional shape formed when a carbon atom is bonded to four other atoms, resembling a pyramid.

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Harold Urey

Scientist who proposed the possibility of abiotic synthesis of organic compounds.

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Cis Isomer

A type of geometric isomer where the two attached atoms on the double bonded carbons are on the same side.

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Trans Isomer

A type of geometric isomer where the two attached atoms on the double bonded carbons are on opposite sides.

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Enantiomers

Isomers that are mirror images of each other due to an asymmetric carbon atom.

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Asymmetric Carbon Atom

A carbon atom bonded to four different atoms or groups of atoms.

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Functional group

Specific groups of atoms within molecules that are directly involved in the chemical reactions.

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Organic Compound

Molecule containing carbon; except for carbon dioxide, and carbonates

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Estradiol/Testosterone

Hormones with similar structures different functional groups, with differences in their functional groups that determine the sexual characteristics of the organism.

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Enantiomers example

Methamphetamine has enantiomers with dramatically different effects; one is a stimulus while the other is a less strong stimulant used in inhalers.

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Hydroxyl Group

A chemical group consisting of an oxygen atom bonded to a hydrogen atom, found in many biological molecules.

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Carbonyl Group

A chemical group consisting of a carbon atom double-bonded to an oxygen atom.

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Carboxyl Group

A chemical group consisting of a carbon atom double-bonded to an oxygen atom and also bonded to a hydroxyl group (–OH).

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Amino Group

A chemical group consisting of a nitrogen atom bonded to two hydrogen atoms and the carbon skeleton.

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Sulfhydryl Group

A chemical group consisting of a sulfur atom bonded to a hydrogen atom.

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Phosphate Group

A chemical group consisting of a phosphorus atom bonded to four oxygen atoms.

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Methyl Group

A chemical group consisting of a carbon atom bonded to three hydrogen atoms.

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ATP

Adenosine triphosphate; a nucleotide that stores potential energy in the bonds between its phosphate groups.

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Polymer

A large molecule composed of repeating structural units (monomers) connected by covalent bonds.

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Monomer

A small molecule that serves as a building block for a polymer.

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Polymerization

The process of forming a polymer from monomers.

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Dehydration Reaction

A chemical reaction in which two molecules are joined by a covalent bond with the removal of a water molecule.

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Hydrolysis

A chemical process in which a molecule is broken into two smaller molecules by the addition of a water molecule.

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Enzyme

A biological catalyst that speeds up chemical reactions.

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Macromolecule

A very large molecule, typically formed by the joining of many smaller molecules.

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Monosaccharide

The simplest carbohydrate; a monomer from which more complex carbohydrates are built. Their formulas usually involve some variation or multiple of CH2O.

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Disaccharide

Two monosaccharides joined by a covalent bond (glycosidic linkage).

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Polysaccharide

A carbohydrate polymer composed of many monosaccharides linked together by glycosidic linkages.

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Glucose

A common monosaccharide with the formula C6H12O6. It's a primary energy source.

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Glycosidic Linkage

A covalent bond formed between two monosaccharides by a dehydration reaction.

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Starch

A storage polysaccharide in plants, composed of glucose monomers. Plants store starch in plastids.

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Glycogen

A storage polysaccharide in animals, composed of branched glucose monomers.

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Cellulose

A structural polysaccharide in plants, composed of glucose monomers arranged differently than in starch.

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Lipid

A class of hydrophobic biological molecules that don't form true polymers.

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Fatty Acid

A long hydrocarbon chain with a carboxyl group at one end. Forms part of a fat molecule.

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Saturated Fat

A fat with no double bonds in its hydrocarbon chains.

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Unsaturated Fat

A fat with one or more double bonds in its hydrocarbon chains.

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Triacylglycerol

Another name for fat; a glycerol molecule joined to three fatty acids.

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Ester Linkage

A bond formed between a hydroxyl group and a carboxyl group during the synthesis of a fat.

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What is a phospholipid?

A major component of cell membranes with a structure similar to fats but with only two fatty acids and a phosphate group attached to glycerol.

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What are the two ends of a phospholipid?

Phospholipids have a hydrophilic head, which loves water, and two hydrophobic tails, which hate water.

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Phospholipid Bilayer

A double layer of phospholipids where the hydrophobic tails are hidden and the hydrophilic heads point outward.

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What does the phospholipid bilayer do?

The phospholipid bilayer acts as a boundary between the cell and its external environment.

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What are steroids?

Lipids characterized by a carbon skeleton forming four fused rings.

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Cholesterol

A common steroid found in animal cell membranes and the base molecule for other steroids.

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What is the danger of high cholesterol?

High levels of cholesterol can contribute to atherosclerosis (plaque buildup in blood vessels)

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What are the types of fat?

There are two main types of fat: saturated fat and unsaturated fat.

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What is a cis double bond?

A double bond where the hydrogen atoms are on the same side of the carbon chain, causing a bend.

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Trans Fat

Unsaturated fats with trans-double bonds, meaning the hydrogen atoms are on opposite sides of the carbon chain creating a straight molecule.

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What are the dangers of trans fat?

Trans fats contribute to coronary heart disease.

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What are lipids?

A class of hydrophobic (water-hating) biological molecules that are generally not polymers.

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Alpha Helix

A secondary structure in proteins where the polypeptide chain coils into a helix shape, stabilized by hydrogen bonds between every fourth amino acid.

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Beta Pleated Sheet

A secondary structure in proteins where polypeptide chains lie side-by-side, forming flat sheets stabilized by hydrogen bonds between adjacent strands.

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Tertiary Structure

The three-dimensional shape of a single polypeptide chain, determined by interactions between side chains of amino acids.

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Hydrophobic Interaction

A type of interaction in protein folding where nonpolar amino acids cluster together in the protein's interior, avoiding contact with water.

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Quaternary Structure

The arrangement and interactions of multiple polypeptide chains (subunits) in a protein complex.

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Disulfide Bridge

A strong covalent bond formed between two cysteine amino acids in a protein, helping to stabilize its tertiary structure.

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Sickle Cell Disease

A genetic disorder caused by a single amino acid substitution in the hemoglobin protein, leading to abnormal sickle-shaped red blood cells.

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Folding of Polypeptide Chains

The process of a polypeptide chain attaining its specific three-dimensional structure, driven by interactions between amino acid side chains and the crowded environment of the cell.

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Secondary Structure

The coiling and folding of a protein molecule, forming structures like alpha helices and beta pleated sheets. This is primarily held together by hydrogen bonds within the polypeptide backbone.

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Denaturation

The process of a protein losing its 3D structure due to changes in environmental factors like pH, temperature, or salt concentration.

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Protein Folding

The process where a polypeptide chain folds into a specific 3D shape, guided by interactions between its amino acids.

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Misfolded Proteins

Proteins that don't fold correctly, leading to loss of function and accumulation that can cause diseases like Alzheimer's and cystic fibrosis.

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X-ray Crystallography

A technique used to determine the 3D structure of proteins by analyzing the diffraction pattern of X-rays passing through a crystal of the protein.

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Intrinsically Disordered Proteins

Proteins that don't have a fixed 3D structure until they interact with other molecules. This flexibility allows them to bind to different partners.

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Polypeptide

A linear chain of amino acids linked by peptide bonds.

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Amino Acid

The building block of proteins, consisting of a central carbon atom bonded to an amino group, a carboxyl group, a hydrogen atom, and a side chain.

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Side Chain (R Group)

The variable part of an amino acid that gives it its unique properties.

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Peptide Bond

A covalent bond that links two amino acids together, formed by a dehydration reaction.

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Primary Structure

The linear sequence of amino acids in a polypeptide chain.

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Adipose Cells

Specialized cells in mammals that store long-term food reserves in the form of fat. They swell and shrink as fat is deposited and withdrawn.

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Phospholipid Structure

A molecule with two fatty acid tails attached to glycerol, with a phosphate group carrying a charge attached to the third hydroxyl group.

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Steroids

Lipids with a carbon skeleton forming four fused rings. Different steroids have different chemical groups attached.

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Atherosclerosis

A condition where high cholesterol levels in the blood can lead to plaque buildup in arteries.

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Catalyst

A substance that speeds up a chemical reaction without being consumed in the process.

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Protein Structure

Proteins have four levels of structure: primary, secondary, tertiary, and quaternary.

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Protein Denaturation

The process where a protein loses its 3D shape and function due to changes in environmental factors such as pH, temperature, or salt concentration.

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Why Proteins Denature

Denaturation occurs due to the breaking of weak bonds within a polypeptide chain, disrupting its structure.

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Hydrophobic Regions

In a nonpolar solvent, the hydrophobic regions of a denatured protein will face outwards because they are repelled by water.

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Nucleic Acid

A complex organic molecule (polymer) made up of nucleotides that carries genetic information.

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DNA vs. RNA

Both are nucleic acids, but DNA is a double helix and contains thymine (T), while RNA is single-stranded and contains uracil (U) instead.

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Gene Expression

The process where information from a gene is used to create a functional product, usually a protein.

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Central Dogma of Molecular Biology

The flow of genetic information from DNA to RNA to protein.

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Nucleotide

The basic building block of nucleic acids, composed of a sugar, a nitrogenous base, and a phosphate group.

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Nitrogen Bases

The four bases in DNA are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, thymine is replaced with uracil (U).

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Purines and Pyrimidines

Purines are double-ringed bases (A, G), while pyrimidines are single-ringed (C, T/U).

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DNA Structure

DNA consists of two strands of nucleotides that wrap around each other in a double helix, with complementary bases pairing (A-T, C-G).

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RNA Structure

RNA is usually single-stranded and can fold into different shapes, providing versatility in its function.

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Study Notes

Organic Chemistry and Biological Molecules

  • Organic chemistry is the study of carbon-containing substances.
  • Harold Urey proposed abiotic synthesis of organic compounds, potentially a source of life.
  • Carbon forms four bonds, enabling diverse organic compounds.

Carbon's Versatile Structure

  • Carbon atoms have four valence electrons, allowing for branching and intersections.
  • Tetrahedral shape results when carbon is bonded to four atoms.
  • Carbon double bonds maintain a planar structure.
  • Carbon dioxide (O=C=O) is crucial for plant life.
  • Urea (CO(NH2)2) is an example of a carbon-containing organic compound.
  • Chains/skeletons of carbon atoms provide space for other atoms.
  • Hydrocarbons (carbon and hydrogen) are found in petroleum and some biological molecules like fats.
  • Fats and petroleum are hydrophobic due to nonpolar hydrocarbon structures.
  • Fats store high energy.

Isomers

  • Isomers have the same atoms but different structures, hence different properties.
  • Structural isomers differ in covalent arrangement (e.g., straight vs. branched chains).
  • The number of structural isomers increases rapidly with the carbon skeleton size.
  • Cis-trans isomers (geometric isomers) have different arrangements around double bonds.
  • Cis isomers have the same groups on the same side.
  • Trans isomers have the same groups on opposite sides.
  • Enantiomers are mirror-image isomers due to an asymmetric carbon atom.
  • Enantiomers often have different biological effects.

Functional Groups

  • Functional groups are chemicals involved in reactions, influencing molecule properties.
  • The prominent functional groups in biological processes are hydroxyl, carbonyl, carboxyl, amino, sulfhydryl, phosphate, and methyl.
  • Methyl groups are nonpolar and act as tags.
  • Hydrophilic groups (all but sulfhydryl) increase water solubility.
  • Phosphate groups are crucial in ATP.
  • ATP (adenosine triphosphate) stores energy in phosphate bonds.
  • ATP releases energy when a phosphate is removed.

Macromolecules

  • Macromolecules are large molecules.
  • Polymers are chains of repeating monomers linked by covalent bonds.
  • Monomers are repeating units that make up polymers.
  • Polymerization is the process of forming polymers.
  • Enzymes speed up chemical reactions.
  • Condensation reactions build polymers by losing a small molecule.
  • Dehydration reactions are condensation reactions that lose water.
  • Hydrolysis breaks down polymers by adding water.
  • Enzymes are crucial to hydrolysis in digestion.

Carbohydrates

  • Carbohydrates are sugars (polymers of simpler sugars).
  • Disaccharides are two monosaccharides joined.
  • Polysaccharides are complex carbohydrates.
  • Monosaccharides are simple sugars (e.g., glucose, formula C6H12O6).
  • Sugars are often classified as aldose or ketose based on carbonyl position.
  • Sugars are also classified by carbon skeleton size (triose, pentose, hexose).
  • Monosaccharides form rings (more stable).
  • Disaccharides are broken down to monosaccharides for energy.
  • Polysaccharides store or build structures.
  • Starch stores glucose in plants (unbranched or branched).
  • Glycogen stores glucose in animals; extensively branched.
  • Cellulose builds plant cell walls; straight chains, strong hydrogen bonds.
  • Chitin is a structural polysaccharide in arthropod exoskeletons.

Lipids

  • Lipids are hydrophobic molecules (not true polymers).
  • Fats are large molecules assembled from glycerol and fatty acids.
  • Glycerol is a three-carbon alcohol.
  • Fatty acids have long hydrocarbon chains.
  • Saturated fats have no double bonds.
  • Unsaturated fats have one or more double bonds.
  • Trans fats have unusual double bond configurations.
  • Phospholipids have two fatty acids and a phosphate group; a major component of cell membranes.
  • Steroids have four fused carbon rings (e.g., cholesterol).

Proteins

  • Proteins are made from 20 amino acids in chains (polypeptides).
  • Amino acids have an amino group, carboxyl group, and variable side chain (R).
  • Peptide bonds link amino acids.
  • Polypeptides have a primary structure (amino acid sequence).
  • Secondary structures (𝛼-helix, 𝛽-pleated sheets) are stabilized by hydrogen bonds.
  • Tertiary structure is the overall 3D shape, stabilized by interactions among side chains (hydrophobic interactions, hydrogen bonds, disulfide bridges).
  • Quaternary structure involves multiple polypeptide chains (e.g., in hemoglobin).
  • Denaturation is the loss of protein structure due to environmental changes.
  • Proteins can refold or become permanently denatured.
  • Diseases are related to misfolded proteins.
  • X-ray crystallography determines protein 3D structures.

Nucleic Acids

  • Nucleic acids (DNA and RNA) are polymers of nucleotides.
  • Nucleotides have a sugar, a nitrogenous base, and one or more phosphate groups.
  • DNA has a double helix structure with base pairs (A-T, C-G).
  • RNA has a single-stranded structure with base pairs (A-U, C-G).
  • DNA directs RNA synthesis, which directs protein synthesis.

DNA Sequencing

  • DNA sequencing techniques first developed in the 1970s.
  • The human genome project sequenced the complete human genome in the early 2000s.
  • Bioinformatics significantly reduced genome sequencing time and cost.
  • Similarities in genomes support evolutionary relationships.

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Explore the fascinating world of organic chemistry, focusing on the versatile structure of carbon and its crucial compounds. Understand essential concepts like isomers, hydrocarbons, and their significance in life and energy storage. This quiz will test your knowledge on the foundational principles of organic chemistry.

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