6. Protein folding and stability are important issues that ultimately impact the

Question

6. Protein folding and stability are important issues that ultimately impact the biological function of a protein. For each situation outlined below indicate: (12 points) i. if this most likely alters protein folding or protein stability? ii. what level (or levels) of protein structure this will alter? ii. would the resulting protein (after the reaction or addition occurs) be in the native conformation or denatured? 6a. Molecular chaperones are added into a mixture of proteins 6b. Urea is added to a mixture of proteins For questions 7-12 choose the single best answer by circling the letter of your response. (2 points each). 7. Which of the following would be considered to interact through chemical complementarity? a. an antibody interacting with its antigen b. the amino acids in the hydrophobic core of a globular protein c. the interaction between an enzyme and its substrate all of the above e. a and c only

Explanation / Answer

6a) Chaperones are special protein which stabilize non native proteins( freshly synthesized protein inside cells), helps unfolded protein to fold in proper conformation for activity, and unfold protein during translocation to neucleus for protein systhesis.

i) Most likely it will stabilize the mixture by preventing aggregation of protein molecules [ by preventing exposed hydrophobic sites], if there is any unfolded ( non native) protein in that mixture, chaperone will help those protein to fold correctly for actions.[ research have shown that use of chaperones in in-vitro active protein production for experiment is greatly enhanced ]

ii) It affects the secondary, tertiary, quaternary structures of protein.

ii) The resulting protein will be of native form of protein( it means that chaperone will convert non native protein to native protein by folding them into secondary, tertiary and quaternary structure.)

6b)

i) Urea denatures the protein inside mixture by breaking the di-sulphide bond

ii) It affects the secondary, tertiary, quaternary structures of protein.

iii )Resulted protein will be denatured proteins.

7.

antigen and antibody binding has hydrogen bond, ionic bonds ( chemical property)

Hydrophobic bonds are -- chemical property

Interaction between enzyme and substrate is of covalnet type ( chemical property)

soa nswer is d) all of above.

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