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Question: 26 the nh group on the backbone of a polypeptide...

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26. The NH group on the backbone of a polypeptide is a good hydrogen bond donor. For which amino acid is the NH group not a good hydrogen bond donor? 27. Polypeptide chains are most often crosslinked by a pair of which amino acid? What type of crosslinking occurs? Is this an oxidation or reduction reaction? When the crosslink is complete what is the resulting unit called 28. What are four reasons why its important to know amino acid sequence? 29. Polypeptides have resonance in the backbone, where is resonance seen in the polypeptide backbone 30. Why are polypeptide chains conformationally restricted? 31. Are majority of peptide bonds in proteins in the cis or trans configuration? Why? Peptide bonds between which two amino acids show less preference for the trans configuration? 32. What about the structure of polypeptides allow for protein folding? 33. Single bonds can rotate and these rotations are specified by torsion angles. Which torsion angles correspond to the different single bonds that can rotate? How can we view the allowed torsional angles for different polypeptides and what does it tell us? 34. Would you expect Pro-X peptide bonds to tend to have cis conformations like those of X-Pro bonds? Why? 35. How is alpha helix stabilized? 36. What is the screw sense of most alpha helices found in proteins? 37. How are the NH groups and CO groups bonded in an antiparallel beta sheet? 38. What are the NH and CO groups bonded in a parallel beta sheet? 39. Describe the structure of a reverse turn? 40. Describe an alpha helical coiled coil protein? Give an example? What kind of interactions could stabilize this type of tertiary structure?
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