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BCMB 311 Chapter Notes - Chapter 4: Kinesin, Crystallography, Atp Hydrolysis

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School
UTK
Department
Biochemistry and Cellular and Molecular Biology
Course
BCMB 311
Professor
Parks, Bruce

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Document Summary

Active site - region on the surface of an enzyme that binds to a substrate molecule and catalyzes its chemical transformation. Amino acid sequence - the order of the amino acid subunits in protein chain. Sometimes called the primary structure of a protein. Antibodies - protein produced by the b lymphocytes in response to a foreign molecule or invading organism. Binds to the foreign molecule or cell extremely tightly, thereby inactivating it or marking it for destruction. Binding site - region on the surface of a protein, typically a cavity or groove, that interacts with another molecule (a ligand) through the formation of multiple nonequivalent bonds. C-terminus - the end of a polypeptide chain that carries a free carboxyl group. Chromatography - technique used to separate the individual molecules in a complex mixture on the basis of their size, charge, or their ability to bind to a particular chemical group.

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Related Questions

A change in the primary sequence of a protein will never change how a protein is allosteric regulated.a.) Trueb.) FalseWhich of the following is NOT a mechanism of enzyme regulation?a.) Feedback inhibition by a product.b.) Addition or removal of phosphate groups to amino acids with alcohol groups.c.) Stimulation by a substrate or product.d.) Proteolytic cleavage.e.) Removal of a methyl group from the side chain of alanine.Which of these is NOT true about the active site of an enzyme?a.) It is composed of distinct amino acids that perform catalytic activitiesb.) It often has a prosthetic group depending on the enzymec.) It is formed by the folding of the proteind.) It is the site of binding of a competitive inhibitore.) It will never be affected by changes in the primary structure of the pWhich is NOT true about the Km of an enzyme:a.) is calculated as half of the maximal velocity of an enzymeb.) is a hypothetical number that cannot be achieved experimentallyc.) is negatively affected by a competitive inhibitord.) is a measure of how tightly an enzyme binds to its substratee.) all of the above are trueWhich is true about Vmax:a.) is the maximal velocity at which an enzyme can functionb.) is reduced by a non-competitive inhibitorc.) is determined on a Lineweaver-Burke plot by taking the reciprocal of the y-interceptd.) is low for an enzyme with a low Km and high substrate affinitye.) all of the above