Question

1.The amino acid serine is classified as a(n) _________________________________________________ amino acid.

2.A type of chromatography that fractionates proteins based on differences in their size is ____________________________________ chromatography.

3.

In Anfinsen's experiments on the structure and function of RNase, he found that non-covalent bonds were key in determining the _________________________ structure of the enzyme.

4.

A type of reversible enzyme inhibitor that binds to the active site of an enzyme and prevents the substrate from binding the active site is is called a ___________________________________________________ inhibitor.

5.Chymotrypsin activity includes the formation of an acyl-enzyme intermediate, formed as a result of bond formed between a carbonyl carbon in the polypeptide undergoing cleavage and a hydroxyl oxygen on the side chain of the amino acid _____in the enzyme's active site. Prior to this binding, this amino acid donates a proton from its hydroxyl group to the amino acid____ also found in the enzyme's active site.

Answer 1

1)Polar non essential amino acid

-The arrangement of atoms in molecules helps in determining the polarity of amino acis.

-Serine is polar amino acid due to present of positive and negative charge.

-It is non essential amino acid as human body can synthesize serine on its own.

2)Sieve Chromatography

-In this type of chromatography molecules are separated based on their size.

-Large molecules cannot pass through smaller pores while the smaller molecules can pass through smaller pores.

3)tertiary structure

-RNase experiment showed protein protein interaction and they can regulate protein activity.

-This experiment showed non covalent interacts play important role in structure and protein function.

4)Competitive inhibitor

Competitive inhibitors resembles same as of the substrates and get bind to the active site thus prevent formation of enzyme substrate complex.They have same affinity as of substrate.