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10 Cards in this Set

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  • Back
True or False: The substrate-binding site and catalytic site of active sites are ALWAYS separate, distinct features.
False. There can be some overlapping.
The Michaelis Constant, Km, denotes the substrate concentration at which an enzyme is at ______ of maximal velocity of catalyzing activity.
Half.
What does a small dissociation constant signify?
A strong protein -protein/ligand affinity.
How is a GTPase protein activated? Deactivated?
Activated by GEFs which replace a GDP with a GTP. Deactivated by hydrolysis of GTP.
What proteins increased the hydrolytic activity of GTPase?
GAPs. GTPase activating proteins.
How are proteins dependent on ATP activated and deactivated?
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.
What is separated by SDS-PAGE method?
Proteins.
Outline basic protocol of Western Blotting.
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.
Name the three types of chromatography.
Size Exclusion, Antibody -affinity, and Ion-exchange chromatography.
What separation technique is best for distinguishing two proteins that are similar in mass?
2-D Gel Electrophoresis.