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Large polymers consisting of one or more sequences of amino acid subunits joined by peptide bonds. –Informational macromolecules –Doers in living systems.
Are the primary contributors to the structure and function of living systems at all levels. |
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general term for any molecule which can bind a protein |
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The specific region of a protein to which a ligand binds |
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a chemical bond in which one atom loses an electron to form a positive ion and the other atom gains an electron to form a negative ion |
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weaker attractions between nonpolar regions on the ligand and protein |
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Substrate Level Specificity |
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Binds a single substrate-product pair |
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Bind a closely related group of molecules |
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The strength with which a ligand binds to its binding site. |
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2 influencing Factors:
The concentration of unbound ligand
The affinity of the binding site for the ligand |
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Occurs when two or more ligands can bind to the same binding site.
The biological effects of one ligand can be decreased by the presence of a second ligand. |
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Whenever a ligand binds to a protein, the binding forces alter the protein’s shape. –Changes in shape at a binding site changes the shape in other areas of proteins
Allosteric proteins have more than one binding site. –When a protein contains two binding sites, binding of a ligand to one site can alter the shape |
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1st Site Location of the primary binding event |
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1st Site Location of the primary binding event |
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2nd Site A modulator molecule binds to this site regulating the protein.
Can be an activator or inhibitor |
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2nd Site A modulator molecule binds to this site regulating the protein.
Can be an activator or inhibitor |
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Involves the covalent addition of charged chemical groups to the side chains of the amino acids in a protein. |
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A negatively charged phosphate group is transferred from one molecule to another.
Commonly a phosphate from ATP is transferred to a protein |
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Enzyme that adds a phosphate group to a protein |
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Enzyme that removes a phosphate group from a phosphorylated protein |
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Is the energy input required for a chemical reaction to proceed.
Enzymes decrease the activation energy for the reaction |
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between polar groups on the ligand and protein |
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