f g oin were replaced begalanins in e protein how wwola He etiasy sInachuy to ia
ID: 257835 • Letter: F
Question
f g oin were replaced begalanins in e protein how wwola He etiasy sInachuy to iasich agid alanine e prolein , Houever,norgofor amno wauld move to the oukr Sat face of ye pk n C) y ne is a polar a mino acic which moves to Hle ou Surfate of te prokin,Houee, nor plar aleant would move to the hyd ropnobic center of ke pole ia d)? would haetitie lono eaect because glys,ne falan are buth no polar amino acids. ?4 The in k rachons of prolein that help deemie tleshuce of o pro kin afe atred by dena huraton jektept the a hydrophillc inle rachons of tu les h or the seconday Shucture b) hydogen bond iay or hob.c of tk krtary shuctvre Covalent amino bonds of prima sthuetur ok rachions ol)Explanation / Answer
1) Option 'd' is the correct answer.
It would have little to no effect because alanine and glycine are both non-polar amino acids. Both alanine and glycine are hydrophobic, non-polar amino acids. Also, alanine side-chain in very non-reactive, and is thus rarely directly involved in protein function. Due to their hydrophobic nature, both glycine and aalanine will be sequestered in the center of the protein.
2) Option 'd' is the correct answer.
Denaturation due to heat affects all the weak bonds in a protein structure which results in the breaking of hydrophobic or hydrophillic interactions in tertiary structure as well as hydrogen bonds in secondary structure. Only the covalent peptide bonds of the primary structure are strong enough to survive denaturation process.
Related Questions
Navigate
Integrity-first tutoring: explanations and feedback only — we do not complete graded work. Learn more.