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Lecture 8

Lecture 8 – Protein Structure 1.docx

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Department
Life Sciences
Course
Life Sciences 1a
Professor
Robert Lue
Semester
Fall

Description
Sept 26 – Protein Structure 1: Amino Acids and Peptide Bonds  ­ demo  ▯egg precipitated in boiling water, protein denatured ­ most carbons are trans configurations  ­ cis configuration far less favored because electrons attached to alpha carbons  become too close  ­ non­peptide 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 R­group, 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 
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