BIOCHEM 523 Lecture Notes - Lecture 6: Protein Structure, Amphiphile, Proline
3 Oct 2017
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Biochem423/523 - lecture 6 - primary and secondary protein structure. Any secondary protein structure must obey the following principles: No two atoms should approach one another more closely than is allowed by their van der waals radii (steric restrictions) The six atoms in the peptide amide group must remain coplanar and in the trans configuration, and rotation can only happen in the (phi) (n-alpha c) or (psi) (alpha c-c) Hydrogen bonds (noncovalent bonds) should exist to stabilize the structure. The planarity of peptide bonds and side chain steric constraints limit the allowable conformations of the polypeptide chain. Cleavage of the polypeptide chain at specific residues by using reagents can be used to break down large proteins into smaller pieces where their sequences can be analyzed. For sequence analysis, mass spectrometry has come to the fore in recent years. The amino acids are joined by peptide bonds.
