The amino acid sequence shown below represents a portion of a peptide obtained from a large protein.
Leu(1) His(2) Ile(3) Thr(4) Arg(5) Phe(6) Phe(7) Pro(8) Cys(9) Met(10) Gly(11) Glu(12) Ala(13) Ile(14) Pro(15) His(16) Thr(17) Glu(18) Asp(19) Cys(20) Gln(21) Met(22) Ile(23) His(24) Cys(25) Pro(26) Arg(27) Lys(28) Gln(29) Pro(30) Tyr(31) Leu(32)
Determine where the chain would be more likely to show β bends or reverse turns. Provide a clear explanation for your answer.
Discuss where one would find cross-linked disulfide bonds in this sequence.
Would you consider this molecule to be in an α-helix formation? Explain your answer.
Beta-turns are tight turns stabilized by H-bonds and requiring cis-orientation of amide planes. Proline and glycine are most suited for beta-turns. ...
This solution offers guideline to answer some problems on protein structure.