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Questions and Answers
Which characteristic is true of fatty acid tails?
Which characteristic is true of fatty acid tails?
A fatty acid with multiple double bonds is classified as:
A fatty acid with multiple double bonds is classified as:
What type of lipid has a polar phosphate head group and nonpolar fatty acid tails?
What type of lipid has a polar phosphate head group and nonpolar fatty acid tails?
Which factor does NOT directly affect membrane fluidity?
Which factor does NOT directly affect membrane fluidity?
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What is the main function of high density lipoproteins (HDLs)?
What is the main function of high density lipoproteins (HDLs)?
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Which class of lipids is primarily used as hydrophobic coatings?
Which class of lipids is primarily used as hydrophobic coatings?
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What type of bond connects two monosaccharides to form a disaccharide?
What type of bond connects two monosaccharides to form a disaccharide?
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Which type of lipids are involved in signal transduction, structural support, and cell recognition?
Which type of lipids are involved in signal transduction, structural support, and cell recognition?
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What defines an element?
What defines an element?
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Which of these best describes a polymer?
Which of these best describes a polymer?
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What is the primary difference between ribose and deoxyribose sugars?
What is the primary difference between ribose and deoxyribose sugars?
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What type of reaction is responsible for the formation of phosphodiester bonds between nucleotides?
What type of reaction is responsible for the formation of phosphodiester bonds between nucleotides?
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Which of the following is true about intermolecular forces?
Which of the following is true about intermolecular forces?
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Which of these statements accurately describes the purpose of tRNA?
Which of these statements accurately describes the purpose of tRNA?
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Given the formula for monosaccharides $(CH_2O)_n$, how many carbon atoms are present in a monosaccharide with n=5?
Given the formula for monosaccharides $(CH_2O)_n$, how many carbon atoms are present in a monosaccharide with n=5?
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What process is used to break down polymers into individual monomers using water?
What process is used to break down polymers into individual monomers using water?
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What type of bonds primarily hold together starch and glycogen polysaccharides?
What type of bonds primarily hold together starch and glycogen polysaccharides?
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Which protein structure is characterized by the specific sequence of amino acids?
Which protein structure is characterized by the specific sequence of amino acids?
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What is the role of peptide bonds in proteins?
What is the role of peptide bonds in proteins?
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Which statement is correct regarding the role of a catalyst in a chemical reaction?
Which statement is correct regarding the role of a catalyst in a chemical reaction?
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Which polysaccharide serves as a structural component in plant cells?
Which polysaccharide serves as a structural component in plant cells?
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What is a key characteristic of an enzyme's active site?
What is a key characteristic of an enzyme's active site?
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What happens to a protein when it denatures?
What happens to a protein when it denatures?
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Which of these best describes a holoenzyme?
Which of these best describes a holoenzyme?
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What is primarily accomplished by a phosphatase enzyme?
What is primarily accomplished by a phosphatase enzyme?
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How does a negative feedback loop affect enzyme activity?
How does a negative feedback loop affect enzyme activity?
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In competitive inhibition, what happens when an inhibitor binds to the enzyme?
In competitive inhibition, what happens when an inhibitor binds to the enzyme?
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If a reaction is subject to noncompetitive inhibition, how do $K_M$ and $V_{max}$ change?
If a reaction is subject to noncompetitive inhibition, how do $K_M$ and $V_{max}$ change?
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What effect does competitive inhibition have on $K_M$ and $V_{max}$ of an enzymatic reaction?
What effect does competitive inhibition have on $K_M$ and $V_{max}$ of an enzymatic reaction?
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Flashcards
Enzymes
Enzymes
Biological catalysts that speed up reactions without being consumed.
Active Site
Active Site
The specific region on an enzyme where the substrate binds.
Ribozyme
Ribozyme
A type of enzyme that is made of RNA instead of protein.
Cofactors
Cofactors
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Holoenzyme
Holoenzyme
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Apoenzyme
Apoenzyme
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Inhibitor
Inhibitor
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Vmax
Vmax
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What are polysaccharides?
What are polysaccharides?
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What is starch?
What is starch?
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What is glycogen?
What is glycogen?
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What is cellulose?
What is cellulose?
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What are amino acids?
What are amino acids?
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What is an atom?
What is an atom?
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What is a molecule?
What is a molecule?
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What are intramolecular forces?
What are intramolecular forces?
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What are intermolecular forces?
What are intermolecular forces?
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What is a monomer?
What is a monomer?
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What is polymerization?
What is polymerization?
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What is a polymer?
What is a polymer?
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What is a dehydration reaction?
What is a dehydration reaction?
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Fatty Acid
Fatty Acid
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Unsaturated Fatty Acid
Unsaturated Fatty Acid
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Saturated Fatty Acid
Saturated Fatty Acid
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Triglyceride
Triglyceride
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Phospholipid
Phospholipid
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Membrane Fluidity
Membrane Fluidity
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Cholesterol
Cholesterol
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Lipoprotein
Lipoprotein
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Study Notes
Enzymes
- Catalysts increase reaction rates without affecting equilibrium, reaction direction, or spontaneity.
- Enzymes are biological catalysts, mostly proteins.
- Enzymes have active sites that bind specific substrates to increase reaction rate.
- Active sites exhibit "induced fit," slightly changing shape to accommodate the substrate.
- Ribozymes are non-protein enzymes made of RNA.
- Cofactors are molecules that enhance enzyme function.
- Holoenzymes are enzymes with their cofactors bound.
- Apoenzymes are enzymes without their cofactors.
- Enzymes can catalyze reactions through substrate approach, presence of acids/bases, and electrostatic interactions.
- Phosphatases remove phosphate groups from substrates.
- Phosphorylases add phosphates to substrates via bond breakage.
- Kinases transfer phosphates from ATP to a substrate.
Enzyme Inhibition and Kinetics
- Enzyme activity alteration impacts reaction rates.
- Substrate binding to active or allosteric sites impacts manipulation.
- Positive feedback loops increase reaction.
- Negative feedback loops decrease reaction.
- Molecules bind to allosteric sites influencing enzyme function.
- Competitive inhibitors compete with substrates for the active site.
- Noncompetitive inhibitors bind to allosteric site, altering active site conformation.
- Enzyme kinetics tracks reaction velocities against substrate concentration.
- Vmax is the maximum reaction velocity.
- Km is substrate concentration at half Vmax.
- Competitive inhibition increases Km, preserving Vmax.
- Non-competitive inhibition decreases Vmax, preserving Km.
Lipids
- Lipids primarily consist of carbon, hydrogen, and oxygen.
- Fatty acid tails are hydrophobic hydrocarbon chains.
- Lipids can be hydrophobic, hydrophilic, or amphipathic.
- Saturated fatty acids lack double bonds, whereas unsaturated fatty acids have one or more double bonds.
- Monounsaturated fatty acids have one double bond, while polyunsaturated fatty acids have multiple double bonds.
- Cis and trans configurations affect lipid packing.
- Glycerol backbones hold fatty acids in triglycerides.
- Triglycerides are mostly hydrophobic.
- Phospholipids are amphipathic, with a polar head and nonpolar tails.
- Phospholipids form bilayers in aqueous solutions.
Lipid Subtypes
- Membrane fluidity depends on temperature, cholesterol, and fatty acid unsaturation.
- Cholesterol is a crucial component in steroid hormones, vitamin D, and bile acids.
- Lipoproteins transport cholesterol and proteins in the blood.
- Low-density lipoproteins deposit cholesterol in tissues.
- High-density lipoproteins deliver cholesterol to the liver.
- Waxes are simple hydrophobic protective coatings.
- Carotenoids are long-chain lipids found in pigments.
- Sphingolipids support cell signaling, structure, and recognition.
- Glycolipids are fatty acids attached to carbohydrates, crucial for cell membranes.
Biological Chemistry
- Matter occupies space and possesses mass.
- Elements are pure substances with unique chemical and physical properties.
- Atoms are the fundamental units of matter.
- Molecules are formed when two or more atoms bind.
- Intramolecular forces bond atoms within a molecule.
- Intermolecular forces bond molecules together.
- Monomers are single molecules that combine to form polymers.
- Polymerization bonds monomers into polymers.
- Dehydration (condensation) reactions link monomers, releasing water.
- Depolymerization breaks polymers into monomers.
- Hydrolysis uses water to break polymer bonds.
Nucleic Acids
- Nucleic acids (DNA and RNA) are built from nucleotides.
- Nucleotides consist of a sugar, a nitrogenous base, and phosphate groups.
- RNA molecules are typically single-stranded.
- Ribose sugar is the component of RNA.
- DNA molecules are typically double-stranded.
- Deoxyribose sugar is the component of DNA
- Phosphodiester bonds connect nucleotides together in a chain.
- The backbone of nucleic acids is formed by sugars and phosphates.
- Nucleotides join to create a nucleic acid chain.
- mRNA carries genetic information for protein synthesis.
- tRNA transfers amino acids during protein synthesis.
- rRNA is a component of ribosomes, sites of protein synthesis.
- miRNA and dsRNA regulate gene expression.
Carbohydrates
- Carbohydrates are used for energy and structural support.
- Carbohydrates contain carbon, hydrogen, and oxygen atoms.
- Monosaccharides are simple carbohydrates (e.g., ribose, fructose, glucose).
- Disaccharides are formed by linking two monosaccharides through glycosidic bonds.
- Polysaccharides are complex carbohydrates with many monosaccharides linked through glycosidic bonds.
- Starch is a plant-based storage polysaccharide.
- Glycogen is an animal-based storage polysaccharide.
- Cellulose is a structural polysaccharide found in plant cell walls.
Protein Structure
- Proteins are composed of amino acids linked by peptide bonds.
- There are 20 different amino acids in proteins.
- Primary structure is the linear sequence of amino acids.
- Secondary structure involves local folding patterns (alpha-helices, beta-sheets).
- Tertiary structure is the three-dimensional shape of a single polypeptide chain.
- Quaternary structure involves the arrangement of multiple polypeptide chains to form a protein complex.
- Protein denaturation disrupts higher-level structure, affecting function.
- Proteins have diverse functions (e.g., enzymes, hormones, structural components).
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Description
This quiz covers the fundamental concepts of enzymes, their roles as biological catalysts, and the various mechanisms of enzyme action. Topics include active sites, co-factors, and enzyme kinetics. Test your understanding of these essential biochemical processes!