Organic Chemistry Essentials

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Questions and Answers

Explain how the properties of the R-group of an amino acid contribute to the overall structure and function of a protein. Provide an example.

The R-group's properties (size, charge, polarity) dictate how the amino acid interacts with other molecules and its location within the protein. For example, hydrophobic R-groups tend to cluster in the protein's interior, away from water.

Describe how a condensation reaction and a hydrolysis reaction are related, yet distinct, in the context of polymer formation and breakdown.

Condensation reactions form polymers by removing water molecules, while hydrolysis reactions break down polymers by adding water. They're opposite processes involved in polymer synthesis and degradation.

Explain how the $\alpha$ and $\beta$ orientations of glucose affect the structure and function of polysaccharides like starch versus cellulose.

$\alpha$ glucose linkages in starch create a helical, loosely packed structure digestible by animals. $\beta$ glucose linkages in cellulose form linear, rigid, tightly packed structures indigestible by animals without specific enzymes.

Describe the role of disulfide bridges in the tertiary structure of proteins, including what amino acid is required.

<p>Disulfide bridges, formed between the sulfur atoms of cysteine residues, covalently link different parts of a protein chain, stabilizing its 3D structure.</p> Signup and view all the answers

Explain why lipids are described as hydrophobic and how this property determines their behavior in an aqueous environment.

<p>Lipids are hydrophobic due to their nonpolar hydrocarbon chains. In an aqueous environment, they cluster together to minimize contact with water, leading to phenomena like the formation of lipid bilayers or micelles.</p> Signup and view all the answers

Describe how the arrangement of phospholipids in a bilayer contributes to the selective permeability of cell membranes.

<p>Phospholipids form a bilayer with hydrophobic tails facing inward and hydrophilic heads facing outward. This arrangement creates a barrier that restricts the passage of polar and charged molecules while allowing nonpolar molecules to pass through more easily.</p> Signup and view all the answers

Explain the difference between a saturated and an unsaturated fatty acid, and how this difference affects the physical properties (e.g., solid vs. liquid at room temperature) of the triglycerides they compose.

<p>Saturated fatty acids have no double bonds, allowing tight packing and resulting in solids at room temperature. Unsaturated fatty acids have double bonds, creating kinks that prevent tight packing and resulting in liquids at room temperature.</p> Signup and view all the answers

Describe how moderate heating can affect the different levels of protein structure, and explain why some levels are more sensitive to heat than others.

<p>Moderate heat primarily disrupts secondary and tertiary structures by breaking hydrogen bonds and hydrophobic interactions. Primary structure (peptide bonds) is more resilient unless heating is extreme.</p> Signup and view all the answers

Describe how the size and shape of glycine and proline affect protein folding and flexibility, and explain why they are often found in specific locations within a folded polypeptide.

<p>Glycine's small size increases flexibility in the protein backbone, often found in loops or turns. Proline's rigid cyclic structure introduces kinks and reduces flexibility, generally disrupting alpha helices.</p> Signup and view all the answers

Explain how environmental conditions such as pH and salt concentration can affect protein structure and function.

<p>Changes in pH and salt concentration can disrupt ionic bonds and hydrogen bonds in proteins, leading to denaturation and loss of function. Extreme conditions can cause irreversible unfolding.</p> Signup and view all the answers

Flashcards

Four main classes of organic molecules

Carbohydrates, lipids (or fats), proteins, and nucleic acids.

Isomer Definition

Isomers are molecules with the same molecular formula but different structural arrangements.

Condensation Reaction

A reaction that joins monomers by removing a water molecule.

Positively Charged Amino Acids

Lysine, arginine, and histidine.

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Negatively Charged Amino Acids

Aspartic acid and glutamic acid.

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Disulfide Bridge

A covalent bond derived from the thiol groups of two cysteine amino acids

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Primary Structure of a Protein

A linear sequence of amino acids held together by peptide bonds.

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Secondary Structure of a Protein

The arrangement of the polypeptide chain into structures such as alpha helices and beta-pleated sheets.

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Tertiary Structure of a Protein

Overall three-dimensional structure of a protein, resulting from interactions between amino acid side chains.

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Quaternary Structure of a Protein

A protein complex composed of multiple polypeptide chains or subunits.

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Study Notes

  • Key molecules characteristic of living things: include carbohydrates, lipids, proteins, and nucleic acids
  • Polymers consist of monomers, which are small repeating units that make up larger molecules
  • Important functional groups: hydroxyl (-OH), carbonyl (C=O), carboxyl (-COOH), amino (-NH2), sulfhydryl (-SH), phosphate (-OPO32-), and methyl (-CH3)
  • Functional group properties vary: some are polar, nonpolar, charged (acidic or basic), influencing molecular interactions

Isomers

  • Isomers are molecules with the same molecular formula but different structural arrangements
  • Types of isomers: structural isomers, cis-trans isomers, and enantiomers

Reactions

  • Condensation reaction: a water molecule is released to form a new bond
  • Hydrolysis reaction: a water molecule is consumed to break a bond

Proteins

  • Proteins are polymers composed of amino acid monomers
  • All amino acids contain an amino group and a carboxyl group
  • These groups exist in ionized forms inside cells
  • The L isomer is the form of amino acids observed in organisms
  • Positively charged amino acids: lysine, arginine, and histidine; these are basic and can form ionic bonds
  • Negatively charged amino acids: aspartic acid and glutamic acid; these are acidic and can form ionic bonds
  • Uncharged polar amino acids: serine, threonine, cysteine, tyrosine, asparagine, and glutamine; these can form hydrogen bonds
  • Nonpolar amino acids: alanine, valine, leucine, isoleucine, methionine, phenylalanine, and tryptophan; these associate via hydrophobic interactions
  • Glycine and proline are exceptional amino acids that don't fall into the common categories
  • Disulfide bridge: a covalent bond formed between the sulfhydryl groups of two cysteine amino acids
  • Glycine's small size and proline's rigid cyclic structure affect their location within a folded polypeptide

Polypeptides and Proteins

  • Polypeptide: a chain of amino acids linked by peptide bonds
  • Proteins: consist of one or more polypeptide chains folded into a specific 3D conformation
  • Peptide bonds form by dehydration reactions between the carboxyl group of one amino acid and the amino group of another
  • Primary structure: the sequence of amino acids in a polypeptide chain, stabilized by peptide bonds
  • Secondary structure: local folding patterns like alpha helices and beta-pleated sheets, stabilized by hydrogen bonds between backbone atoms
  • Tertiary structure: the overall 3D shape of a protein, stabilized by various interactions between R groups, including hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges
  • Quaternary structure: the association of multiple polypeptide subunits into a functional protein complex, stabilized by the same interactions as tertiary structure
  • Moderate heating affects secondary and tertiary structures
  • Denatured protein: a protein that has lost its native conformation due to disruption of non-covalent interactions
  • Shape and surface chemistry determine protein function: specific binding sites allow proteins to interact with other molecules
  • Environmental conditions such as temperature, pH, and salt concentration can affect protein structure
  • Interactions with other molecules can affect protein structure by stabilizing specific conformations or inducing conformational changes

Carbohydrates

  • Carbohydrates contain carbon, hydrogen, and oxygen, with functional groups such as hydroxyl and carbonyl
  • Carbohydrates' roles include energy storage, structural support, cell-cell recognition, and precursors for other biomolecules
  • Monosaccharide: a simple sugar (e.g., glucose, fructose)
  • Disaccharide: two monosaccharides joined by a glycosidic bond (e.g., sucrose, lactose)
  • Oligosaccharide: a few (3-10) monosaccharides joined by glycosidic bonds
  • Polysaccharide: many monosaccharides joined by glycosidic bonds (e.g., starch, cellulose)
  • Six-carbon sugar example: glucose
  • Five-carbon sugar example: ribose
  • Alpha orientation of glucose: the hydroxyl group on carbon-1 is below the plane of the ring
  • Beta orientation of glucose: the hydroxyl group on carbon-1 is above the plane of the ring
  • Glycosidic bond formation: a condensation reaction between two monosaccharides
  • Alpha bond: the bond between carbon-1 and carbon-4 is oriented downwards
  • Beta bond: the bond between carbon-1 and carbon-4 is oriented upwards
  • Named glycosidic bond: by numbering the carbons involved and indicating the alpha or beta orientation
  • Three polysaccharides highlighted: starch, glycogen, and cellulose
    • Starch: arranged in helical structure, found in plants, energy storage
    • Glycogen: arranged in helical structure with more branching than starch, found in animals, energy storage
    • Cellulose: arranged linearly, found in plant cell walls, structural support

Lipids

  • Lipids aren't polymers as they do not consist of repeating monomeric units covalently bonded together
  • Lipids are hydrophobic due to their nonpolar hydrocarbon regions
  • Triglyceride structure: glycerol molecule attached to three fatty acids via ester linkages
  • Saturated fatty acid: contains no carbon-carbon double bonds, resulting in a straight chain
  • Unsaturated fatty acid: contains one or more carbon-carbon double bonds, causing kinks in the chain
  • Triglycerides with saturated fatty acids are solid at room temperature, while those with unsaturated fatty acids are liquid
  • Phospholipid components: glycerol molecule attached to two fatty acids and a phosphate group
  • Amphipathic: molecule with both hydrophilic and hydrophobic regions
  • Phospholipids in an aqueous solution: form bilayers with the hydrophobic tails inward and the hydrophilic heads outward

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