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Questions and Answers
What is the primary structural feature that distinguishes proline from other amino acids?
What is the primary structural feature that distinguishes proline from other amino acids?
Which amino acid is responsible for the formation of disulfide bonds in proteins?
Which amino acid is responsible for the formation of disulfide bonds in proteins?
How does the substitution of glutamate with valine in hemoglobin affect its function?
How does the substitution of glutamate with valine in hemoglobin affect its function?
Which of the following amino acids contains a hydroxyl group capable of forming hydrogen bonds?
Which of the following amino acids contains a hydroxyl group capable of forming hydrogen bonds?
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Why is proline often referred to as an imino acid?
Why is proline often referred to as an imino acid?
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At a physiologic pH of approximately 7.4, which amino acid has a side chain that can lose a proton?
At a physiologic pH of approximately 7.4, which amino acid has a side chain that can lose a proton?
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In what manner do the side chains of asparagine and glutamine facilitate protein interactions?
In what manner do the side chains of asparagine and glutamine facilitate protein interactions?
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Which structural feature of collagen is directly influenced by the presence of proline?
Which structural feature of collagen is directly influenced by the presence of proline?
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What role do amino acids play in the formation of proteins?
What role do amino acids play in the formation of proteins?
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What is the state of the carboxyl group of an amino acid at physiologic pH?
What is the state of the carboxyl group of an amino acid at physiologic pH?
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Which of the following correctly describes the amino group in amino acids at physiologic pH?
Which of the following correctly describes the amino group in amino acids at physiologic pH?
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What distinguishes standard amino acids from nonstandard amino acids?
What distinguishes standard amino acids from nonstandard amino acids?
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Which amino acid has a unique structural feature compared to others?
Which amino acid has a unique structural feature compared to others?
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How are amino acids within proteins referred to?
How are amino acids within proteins referred to?
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What happens to the carboxyl and amino groups during peptide bond formation?
What happens to the carboxyl and amino groups during peptide bond formation?
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What determines the functional role of an amino acid in a protein?
What determines the functional role of an amino acid in a protein?
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What type of amino acids has side chains that do not gain or lose protons or participate in hydrogen or ionic bonds?
What type of amino acids has side chains that do not gain or lose protons or participate in hydrogen or ionic bonds?
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In a polar environment, where do nonpolar amino acid side chains typically cluster?
In a polar environment, where do nonpolar amino acid side chains typically cluster?
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What is a key property of nonpolar side chains in amino acids that promotes hydrophobic interactions?
What is a key property of nonpolar side chains in amino acids that promotes hydrophobic interactions?
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At physiologic pH, which of the following amino acid components are typically deprotonated?
At physiologic pH, which of the following amino acid components are typically deprotonated?
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Which phenomenon describes the clustering of nonpolar amino acid side chains in a polar environment?
Which phenomenon describes the clustering of nonpolar amino acid side chains in a polar environment?
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In a hydrophobic environment, where are nonpolar R groups likely to be found?
In a hydrophobic environment, where are nonpolar R groups likely to be found?
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The structure of which amino acid would have a side chain classified as nonpolar?
The structure of which amino acid would have a side chain classified as nonpolar?
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What impact do nonpolar R groups have on the three-dimensional structure of proteins?
What impact do nonpolar R groups have on the three-dimensional structure of proteins?
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Study Notes
Overview of Enzymes
- Enzymes are protein catalysts that speed up chemical reactions in the body.
- They don't change during the reaction.
- Enzymes are very specific, targeting usually one type of reaction.
- Enzymes are crucial for metabolic processes.
Nomenclature
- Enzyme names usually end in "-ase".
- Enzymes have a recommended name (common name) and a systematic name (scientific).
Enzyme Properties
- Active Site: A specific pocket on the enzyme surface where the substrate binds. It is designed to fit that specific substrate closely.
- Efficiency: Enzymes greatly increase reaction rates compared to uncatalyzed reactions.
- Specificity: Enzymes are very specific, typically binding to one type of substrate and catalyzing only one type of reaction.
Enzyme Inhibition
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Reversible Inhibitors:
- Competitive: Inhibitors bind to the active site, competing with the substrate. Increasing substrate concentration reverses the effect.
- Noncompetitive: Inhibitors bind to a different site on the enzyme, changing the enzyme's shape, making it inactive. Higher substrate concentrations don't alter the inhibitory effect.
Enzyme Regulation
- Allosteric Enzymes: Enzymes whose activity is regulated by molecules called effectors that bind to it at a site distinct from the active site.
- Covalent Modification: The activity of many enzymes is regulated by the addition or removal of phosphate groups from amino acid residues.
- Enzyme Synthesis: Regulation of the amount of enzyme present (synthesis or degradation) can also adjust overall enzyme activity.
Enzymes in Blood
- Some enzymes are found within the blood, and their elevated levels in the blood can indicate damage to specific tissues or organs.
- Isoenzymes: Different (slightly varying structural) forms of an enzyme can be separated using electrophoresis. The level of each isoenzyme can be useful in diagnosis.
Hemoglobinopathies
- A group of genetic blood disorders that cause a structurally abnormal hemoglobin or decreased amount of normal hemoglobin production.
- Some are serious, such as sickle cell disease and some are relatively mild.
Other Topics
- pH: Affects enzyme activity (because of the ionic nature of enzyme substrates and amino acids).
- Temperature: Enzyme activity plateaus and then declines with increasing temperature. The optimum temperature generally corresponds to optimal body temperature.
- Michaelis-Menten Kinetics: A mathematical model used to describe enzyme activity.
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