Bioechemistry - Enzymes

Chemistry
Bioechemistry - Enzymes

Sample Data

Front Effect of Uncompetitive Inhibitors on Enzyme Kinetics
Back - bind to enzyme at allosteric site only after enzyme has bound to substrate, and the enzyme will have a lower activity as a result- Since enzyme cannot catalyze at full reaction speed, Vmax is lowered- Since increasing substrate amount can't overcome this effect, it takes less substrate to get to 1/2 of the new Vmax and Km is also lowered 
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Front Types of Protein Structure
Back Primary (1o) - Amino Acid sequenceSecondary (2o) - alpha helices, beta pleated sheets and barrels, random coilsTertiary (3o) - Folding of secondary elements into 3D structureQuaternary (4o) - multiple subunits assembled into larger structure
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Front Beta Pleated Sheets
Back - Intramolecular hydrogen bonds between the parallel or antiparallel strands 
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