to answer the following question. (4 pts) 33) Consider the helical peptide and u
ID: 555950 • Letter: T
Question
to answer the following question. (4 pts) 33) Consider the helical peptide and urea denaturation curve fraction unfolded (wild type) fraction unfolded mutant) 0.8 0.6 Ang 5 0.4 Glu 6 0.2 Arg 15 Glu 1 Glu 1 Arg 10 Glu 11 Arg 10 ureal (M) 15 Glu 6 Arg 15 cH, Ile sidechain: C -CH-CH CH, The three arginine residues (Arg 5, 10, and 15) were all mutated to lle residues and the stability of the mutant was assessed by urea denaturation. Briefly compare... -the relative stabilities of the wild type vs the mutant (which is more stable? which is less stable? Why? (Chint: urea); - the physical basis behind the different stabilities Page 8 of 11Explanation / Answer
33) Urea denaturation experiment and helical peptide
Given above is the graph of amount of protein unfolded (denaturation) versus urea concentration.
- The wild type was found to be more stable when compared to the mutant type derrived from the three arginine residues. The presence of urea changes the pH to basic, which assists in protein defolding or unfolding by breaking the hydrophobic interactions between the arginine residues in the mutant type shown above.
- The physical basis behind the stability is the decreaed hydrophobic interactions between the structures which leads to destabilization of the mutant. The wild type does not have any such complexity and thus show greater hydrophobic interaction and hence higher protein foliding and stability of the structure is greatly improved.
Related Questions
Navigate
Integrity-first tutoring: explanations and feedback only — we do not complete graded work. Learn more.