Proteins - AP Biology
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Identify the protein that acts as a buffer in blood.
Identify the protein that acts as a buffer in blood.
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Albumin. Most abundant blood protein that maintains osmotic pressure.
Albumin. Most abundant blood protein that maintains osmotic pressure.
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Identify the protein responsible for oxygen storage in muscles.
Identify the protein responsible for oxygen storage in muscles.
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Myoglobin. Single-chain protein that stores oxygen in muscle tissue.
Myoglobin. Single-chain protein that stores oxygen in muscle tissue.
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What is the impact of temperature on enzyme activity?
What is the impact of temperature on enzyme activity?
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High temperature can denature enzymes. Extreme heat breaks bonds that maintain enzyme active site.
High temperature can denature enzymes. Extreme heat breaks bonds that maintain enzyme active site.
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What is the role of hemoglobin?
What is the role of hemoglobin?
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Transport oxygen in blood. Iron-containing protein binds and carries oxygen molecules.
Transport oxygen in blood. Iron-containing protein binds and carries oxygen molecules.
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What type of interaction stabilizes tertiary protein structure?
What type of interaction stabilizes tertiary protein structure?
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Hydrophobic interactions, disulfide bridges. Side chain interactions create and maintain 3D protein shape.
Hydrophobic interactions, disulfide bridges. Side chain interactions create and maintain 3D protein shape.
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What is the quaternary structure of proteins?
What is the quaternary structure of proteins?
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Assembly of multiple polypeptide chains. Multiple polypeptides combine to form functional protein complexes.
Assembly of multiple polypeptide chains. Multiple polypeptides combine to form functional protein complexes.
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What is the function of antibodies?
What is the function of antibodies?
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Bind to antigens to neutralize them. Y-shaped proteins that recognize and bind specific foreign substances.
Bind to antigens to neutralize them. Y-shaped proteins that recognize and bind specific foreign substances.
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Which structure is the sequence of amino acids in a polypeptide?
Which structure is the sequence of amino acids in a polypeptide?
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Primary structure. Foundation level that determines all higher structural levels.
Primary structure. Foundation level that determines all higher structural levels.
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Identify one example of a fibrous protein.
Identify one example of a fibrous protein.
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Collagen. Structural protein with elongated, rope-like quaternary structure.
Collagen. Structural protein with elongated, rope-like quaternary structure.
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What is the monomer unit of proteins?
What is the monomer unit of proteins?
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Amino acids. Basic building blocks that link together to form protein chains.
Amino acids. Basic building blocks that link together to form protein chains.
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Identify the bond that links amino acids in proteins.
Identify the bond that links amino acids in proteins.
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Peptide bond. Covalent bond formed by dehydration synthesis between amino acids.
Peptide bond. Covalent bond formed by dehydration synthesis between amino acids.
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What is the role of ferritin?
What is the role of ferritin?
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Stores iron in cells. Storage protein that safely sequesters iron for cellular use.
Stores iron in cells. Storage protein that safely sequesters iron for cellular use.
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Identify the protein responsible for oxygen storage in muscles.
Identify the protein responsible for oxygen storage in muscles.
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Myoglobin. Single-chain protein that stores oxygen in muscle tissue.
Myoglobin. Single-chain protein that stores oxygen in muscle tissue.
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What determines the primary structure of a protein?
What determines the primary structure of a protein?
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Amino acid sequence. Linear order of amino acids determines all higher-level structures.
Amino acid sequence. Linear order of amino acids determines all higher-level structures.
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What is the function of rhodopsin?
What is the function of rhodopsin?
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Photoreceptor protein in the retina. Light-sensitive protein that initiates vision in rod cells.
Photoreceptor protein in the retina. Light-sensitive protein that initiates vision in rod cells.
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What is denaturation in proteins?
What is denaturation in proteins?
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Loss of structure and function. Disruption of non-covalent bonds destroys protein's native shape.
Loss of structure and function. Disruption of non-covalent bonds destroys protein's native shape.
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What is the role of insulin?
What is the role of insulin?
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Regulates blood glucose levels. Hormone that lowers blood sugar by promoting glucose uptake.
Regulates blood glucose levels. Hormone that lowers blood sugar by promoting glucose uptake.
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Identify a method to separate proteins based on size.
Identify a method to separate proteins based on size.
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Gel electrophoresis. Separates proteins by molecular weight through porous gel matrix.
Gel electrophoresis. Separates proteins by molecular weight through porous gel matrix.
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Identify the technique used to determine protein structure.
Identify the technique used to determine protein structure.
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X-ray crystallography. Uses X-rays to reveal atomic-level protein structure details.
X-ray crystallography. Uses X-rays to reveal atomic-level protein structure details.
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What is the quaternary structure of proteins?
What is the quaternary structure of proteins?
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Assembly of multiple polypeptide chains. Multiple polypeptides combine to form functional protein complexes.
Assembly of multiple polypeptide chains. Multiple polypeptides combine to form functional protein complexes.
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What type of interaction stabilizes tertiary protein structure?
What type of interaction stabilizes tertiary protein structure?
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Hydrophobic interactions, disulfide bridges. Side chain interactions create and maintain 3D protein shape.
Hydrophobic interactions, disulfide bridges. Side chain interactions create and maintain 3D protein shape.
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Identify one example of a globular protein.
Identify one example of a globular protein.
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Hemoglobin. Compact, spherical protein with complex tertiary structure.
Hemoglobin. Compact, spherical protein with complex tertiary structure.
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Identify a protein involved in cell signaling.
Identify a protein involved in cell signaling.
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Receptors. Membrane proteins that detect and respond to chemical signals.
Receptors. Membrane proteins that detect and respond to chemical signals.
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What is the role of elastin?
What is the role of elastin?
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Provides elasticity to tissues. Allows tissues to stretch and return to original shape.
Provides elasticity to tissues. Allows tissues to stretch and return to original shape.
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Which enzyme is involved in DNA replication?
Which enzyme is involved in DNA replication?
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DNA polymerase. Synthesizes new DNA strands during cell division.
DNA polymerase. Synthesizes new DNA strands during cell division.
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What is a protein domain?
What is a protein domain?
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Functional unit within a protein. Independently folded region with specific structure and function.
Functional unit within a protein. Independently folded region with specific structure and function.
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What is the role of myosin?
What is the role of myosin?
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Motor protein involved in muscle contraction. Converts chemical energy to mechanical force for movement.
Motor protein involved in muscle contraction. Converts chemical energy to mechanical force for movement.
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Which amino acid has a sulfur atom in its side chain?
Which amino acid has a sulfur atom in its side chain?
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Cysteine. Only amino acid capable of forming disulfide bonds.
Cysteine. Only amino acid capable of forming disulfide bonds.
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Identify a protein involved in immune response.
Identify a protein involved in immune response.
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Antibodies. Immunoglobulins that provide specific defense against pathogens.
Antibodies. Immunoglobulins that provide specific defense against pathogens.
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Which bond is formed between the carboxyl and amino group of two amino acids?
Which bond is formed between the carboxyl and amino group of two amino acids?
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Peptide bond. Dehydration reaction creates covalent linkage in protein backbone.
Peptide bond. Dehydration reaction creates covalent linkage in protein backbone.
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