BIOSC 1000 Lecture Notes - Lecture 5: Guanidinium Chloride, Mhc Multimer, 2-Mercaptoethanol

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Primary protein structure is the amino acid sequence from amino- to carboxyl- terminus. Secondary structure is the local spatial arrangement of a polypeptide"s backbone atoms in a segment of the peptide chain does not take into account the conformations of side chains repeating patterns dictated by bond angles (peptide bond has resonance) The planar nature of peptide bonds constrains the conformation of a polypeptide chain every peptide bond has a phi/psi angle. The trans orientation around a peptide bond is favored the trans orientation has less steric hindrance than the cis orientation. Proline and glycine are the two amino acids that adopt the cis conformation. Glycine is in the cis orientation does not have much hindrance because r group is just an h. Proline cyclizes back on itself and forces itself a cis conformation. There is free rotation about the other bonds in a polypeptide backbone. C(alpha)-nh angle is the phi angle - amino group.

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