THE STRUCTURE AND FUNCTION OF MACROMOLECULES
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| 8393884890 | enzyme | A macromolecule serving as a catalyst, a chemical agent that changes the rate of a reaction without being consumed by the reaction. |  | 0 |
| 8393884891 | polypeptide | A polymer (chain) of many amino acids linked together by peptide bonds. |  | 1 |
| 8393884892 | protein | A functional biological molecule consisting of one or more polypeptides folded and coiled into a specific three-dimensional structure. | 2 | |
| 8393884893 | amino acid | An organic molecule possessing both carboxyl and amino groups. Amino acids serve as the monomers of polypeptides. |  | 3 |
| 8393884894 | peptide bond | The covalent bond between the carboxyl group on one amino acid and the amino group on another, formed by a dehydration reaction. | 4 | |
| 8393884895 | primary structure | The level of protein structure referring to the specific sequence of amino acids. |  | 5 |
| 8393884896 | secondary structure | The localized, repetitive coiling or folding of the polypeptide backbone of a protein due to hydrogen bond formation between constituents of the backbone. | 6 | |
| 8393884897 | Alpha helix | A spiral shape constituting one form of the secondary structure of proteins, arising from a specific pattern of hydrogen bonding. |  | 7 |
| 8393884898 | Beta pleated sheet | One form of the secondary structure of proteins in which the polypeptide chain folds back and forth. Two regions of the chain lie parallel to each other and are held together by hydrogen bonds. |  | 8 |
| 8393884899 | tertiary structure | Irregular contortions of a protein molecule due to interactions of side chains involved in hydrophobic interactions, ionic bonds, hydrogen bonds, and disulfide bridges. |  | 9 |
| 8393884900 | disulfide bridges | A strong covalent bond formed when the sulfur of one cysteine monomer bonds to the sulfur of another cysteine monomer. |  | 10 |
| 8393884901 | quaternary structure | The particular shape of a complex, aggregate protein, defined by the characteristic three-dimensional arrangement of its constituent subunits, each a polypeptide. |  | 11 |
| 8393884902 | denaturation | In proteins, a process in which a protein unravels and loses its native shape, thereby becoming biologically inactive; in DNA, the separation of the two strands of the double helix. Denaturation occurs under extreme (noncellular) conditions of pH, salt concentration, and temperature. |  | 12 |
| 8393884903 | chaperonin | A protein molecule that assists in the proper folding of other proteins. |  | 13 |
| 8393884909 | active site | The specific portion of an enzyme that attaches to the substrate by means of weak chemical bonds. | 14 | |
| 8393884910 | enzyme substrate | The reactant that an enzyme acts on | 15 | |
| 8393884911 | catalyst | (chemistry) a substance that initiates or accelerates a chemical reaction without itself being affected | 16 | |
| 8393884912 | induced-fit model | Theory that suggests that when an enzyme and a substrate bind together, the enzyme is induced to alter its shape for a tighter active-site/substrate attachment, which places the substrate in a favorable position to react more quickly. | 17 | |
| 8393884913 | Cofactors | Minerals that assist in the normal functioning of enzymes | 18 | |
| 8393884914 | coenzymes | vitamins that assist in the normal functioning of enzymes | 19 | |
| 8393884915 | allosteric enzymes | The modification of enzyme activity through interactions of molecules with specific sites on the enzyme other than the active site (called allosteric sites) | 20 | |
| 8393884916 | feedback inhibition | A method of metabolic control in which the end product of a metabolic pathway acts as an inhibitor of an enzyme within that pathway. | 21 | |
| 8393884917 | competitive inhibition | Inhibition of an enzyme's ability to catalyze a chemical reaction via a non-reactant molecule that competes with the substrate(s) for access to the active site. | 22 | |
| 8393884918 | noncompetitive inhibition | A substance that reduces the activity of an enzyme by binding to a location remote from the active site, changing its conformation so that it no longer binds to the substrate. | 23 |
