Proteins quiz #2 Flashcards
Proteins quiz #2
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What is the typical size range of proteins in terms of amino acids? Proteins typically range from 100 to several thousand amino acids. What is the main difference between a polypeptide and a protein? A polypeptide is a single amino acid chain, while a protein is a functional molecule that may consist of one or more polypeptides. What is the function of enzymes in biological systems? Enzymes catalyze and speed up chemical reactions necessary for life. How do substrates interact with enzymes? Substrates fit into the enzyme's active site, forming an enzyme-substrate complex. What happens to substrates during an enzyme-catalyzed reaction? Enzymes convert substrates into products during the reaction. Can enzymes be used repeatedly? Yes, enzymes can be reused for multiple reactions because they are not consumed. Why are enzymes essential for life? Enzymes are essential because they catalyze nearly all cellular reactions at rates necessary for life. What is the significance of the '-ase' suffix in biochemistry? The '-ase' suffix indicates that a molecule is an enzyme. What is a peptidase? A peptidase is an enzyme that breaks down peptides into smaller fragments. What is the relationship between protein structure and function? A protein's structure determines its specific function in the cell. What is the role of the R group in amino acids? The R group gives each amino acid its unique properties and influences protein structure. How are proteins classified based on their structure? Proteins are classified by their primary, secondary, tertiary, and quaternary structures. What is the importance of the primary structure of a protein? The primary structure determines the protein's final shape and function. What types of bonds stabilize secondary protein structures? Hydrogen bonds stabilize secondary structures like alpha helices and beta sheets. What types of interactions stabilize tertiary protein structure? Tertiary structure is stabilized by interactions such as hydrogen bonds, ionic bonds, disulfide bridges, and hydrophobic interactions. What is a protein subunit? A protein subunit is a single polypeptide chain that can associate with others to form a functional protein. What is a functional protein? A functional protein is a polypeptide or group of polypeptides folded into a specific three-dimensional shape that performs a biological function. What is the difference between a substrate and a product in enzyme reactions? A substrate is the molecule acted upon by an enzyme, while a product is the molecule produced by the reaction. What is the significance of the enzyme-substrate complex? The enzyme-substrate complex allows the enzyme to catalyze the conversion of substrate to product efficiently. What is the role of hydrogen bonding in protein structure? Hydrogen bonding helps stabilize secondary and tertiary structures in proteins. What is the role of disulfide bridges in proteins? Disulfide bridges are covalent bonds that help stabilize the tertiary and quaternary structures of proteins. What is the role of hydrophobic interactions in protein folding? Hydrophobic interactions help drive the folding of proteins by causing nonpolar side chains to cluster away from water. What is the role of ionic bonds in protein structure? Ionic bonds between charged side chains help stabilize tertiary and quaternary protein structures. What is the difference between a monomer and a polymer in the context of proteins? A monomer is a single amino acid, while a polymer is a chain of amino acids (a polypeptide or protein). What is the general function of structural proteins? Structural proteins provide support and shape to cells and tissues. What is the general function of regulatory proteins? Regulatory proteins control cellular processes and gene expression. What is the general function of transport proteins? Transport proteins move molecules across cell membranes or within the body. What is the general function of signaling proteins? Signaling proteins transmit signals to coordinate biological processes. What is the general function of defensive proteins? Defensive proteins protect the body from pathogens, such as antibodies. What is the general function of storage proteins? Storage proteins store amino acids or other substances for later use. What is the general function of motor proteins? Motor proteins generate movement within cells and tissues. What is the general function of receptor proteins? Receptor proteins receive and respond to chemical signals. What is the general function of enzymatic proteins? Enzymatic proteins catalyze biochemical reactions. What is the relationship between protein denaturation and function? Denaturation disrupts protein structure, leading to loss of function. What can cause protein denaturation? Protein denaturation can be caused by heat, pH changes, or chemicals. What is the significance of protein folding? Proper protein folding is essential for correct function. What is a chaperone protein? A chaperone protein assists in the proper folding of other proteins. What is the difference between fibrous and globular proteins? Fibrous proteins are long and structural, while globular proteins are compact and functional. What is a prosthetic group in a protein? A prosthetic group is a non-protein component required for protein function. What is a holoenzyme? A holoenzyme is a complete, active enzyme with its necessary cofactors or prosthetic groups.
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