Life Sciences 1a Lecture 8: Lecture 8 – Protein Structure 1.docx

• School: Harvard University
• Department: Life Sciences
• Course: Life Sciences 1a
• Professor: Robert Lue

Document Summary

Most carbons are trans configurations most favorable interactions cis configuration far less favored because electrons attached to alpha carbons become too close non peptide bonds free to rotate so r groups play major role in 3d structure study amino acids and side chains amino acids with nonpolar side chains in interior of proteins amino acids can be modified to change structure and function acidic or basic ones exist primarily in protonated or deprotonated state under physiological conditions glycine does not have r group, achiral, accommodating because not having a side chain makes it more flexible proline side group connected in covalent bond to n, trans isomers only slightly favored over cis isomer because both configurations create unfavorable interactions, can not hydrogen bond to other groups.