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1. T/F: Molecular interactions at binding sites are primarily due to noncovalent

ID: 148166 • Letter: 1

Question

1. T/F: Molecular interactions at binding sites are primarily due to noncovalent interactions. 2. T/F: Differential centrifugation can be used to separate ribosomes from nuclei. 3. T/F: Sandwich ELISAs detect antibodies in a sample, while indirect ELISAs detect antigens. 4. T/F: Enzymes speed up energetically favorable reactions. 5. T/F: Amino acid side chains primarily affect a protein's secondary structure. 6. T/F: Phosphate groups can be added to molecules by phosphatases. 7. T/F: Given a reaction where Vmax 35mmol/hr, if you add 4 times more of the enzyme to the reaction the Vmax will remain the same 8. T/F: As a rule of thumb, phosphorylation of a protein increases its activity. T/FE: When controlling a protein's activty through feedback inhibition, regulatory molecules bind 10. T/F: If the y intercept of a Lineweaver Burk plot is at 3 min/umol, the Vmax is 0.33 umol/min. 11. T/F: An equilibrium constant is calculated by dividing the reactant concentration by the product 12. T/F: In separating proteins using size-exclusion chromatography, small proteins would be found 9. to active sites. concentration. in the later fractions.

Explanation / Answer

Answer 1.

True.

Molecular interactions at binding sites are primerly due to non covalent interations.

Molecular interations are very specific and these interactions are achived by non-covalent weak interaction between the molecules ,these molecules may interact by hydrogen bond or by some ionic interactions between charged molecules or hydrophobic interaction or these can be van der waals interactions. All are types of non covalent interactions, eg. antigen- antibody interactions.