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10 Cards in this Set
- Front
- Back
True or False: The substrate-binding site and catalytic site of active sites are ALWAYS separate, distinct features.
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False. There can be some overlapping.
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The Michaelis Constant, Km, denotes the substrate concentration at which an enzyme is at ______ of maximal velocity of catalyzing activity.
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Half.
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What does a small dissociation constant signify?
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A strong protein -protein/ligand affinity.
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How is a GTPase protein activated? Deactivated?
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Activated by GEFs which replace a GDP with a GTP. Deactivated by hydrolysis of GTP.
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What proteins increased the hydrolytic activity of GTPase?
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GAPs. GTPase activating proteins.
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How are proteins dependent on ATP activated and deactivated?
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Activated by ATP hydrolysis by Protein kinases, which add the P to the protein. Deactivated by Protein phosphotases, which remove the P(i) from the active molecule.
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What is separated by SDS-PAGE method?
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Proteins.
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Outline basic protocol of Western Blotting.
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1st: SDS-PAGE is perfomed. 2nd, Antibody 1 (AB1) is binds to particular proteins. AB2 binds to AB1. Enzyme or other distinguishing substance covalently binds to AB2.
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Name the three types of chromatography.
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Size Exclusion, Antibody -affinity, and Ion-exchange chromatography.
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What separation technique is best for distinguishing two proteins that are similar in mass?
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2-D Gel Electrophoresis.
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