BIO-0013 Lecture : 3.2, 3.3 Class Notes.docx
29 Mar 2014
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Distance between: c n (cid:224) 1. 43 , c=n (cid:224) 1. 25 , peptide bond (cid:224) 1. 33 (partial double bond characteristic) Secondary structure short range folding patterns of the polypeptide chain: right handed a helix, r groups are projected out to the space outside of the helix (cid:224) critical for tertiary structure, beta pleated sheet, conformation is determined by the phi and psi angles, but strands can be stabilized by hydrogen bonds between strands, creating sheets, in beta sheets, the r groups project above and below the plane of the sheet, dictated by angles of phi and psi, stabilized by hydrogen bonds between different amino acids (in polypeptide backbone, not r groups, n h o=c, can be depicted in ribbon diagrams, need to show direction to determine n and c terminus ends, a protein"s secondary structure increases its stability although each hydrogen bond is very weak relative to a covalent bond, the large number of hydrogen bonds makes these structures stable.
