By Erhard Gross
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Additional resources for The Peptides: Analysis and Synthesis. Volume 4
Sample text
In one crystal, the cavity is filled with dimethyl sulfoxide (DMSO) and the lipophilic groups of DMSO are directed toward the polar lining of the cavity, and, in the other case, the cavity contains four water molecules that form strong hydrogen bonds with each other and with the surrounding peptide molecules (Karle and Flippen-Anderson, 1978; Karle, 1976). A number of substances of the ferrichrome family, containing three hydroxamic acid groups coordinated to a central ferric ion, have been isolated, mainly from microbial sources.
1972). , 1979b) are quite asymmetric, and each contains only one 4 -• 1 type II hydrogen bond. In the hexadepsipeptide cyc/o(LVal-LMeIle-DHyv)2 (Shishova and Simonov, 1976), which has an approximate twofold symmetry axis and two intramolecular Ν Η · · * 0 = C bonds that encompass the LMelle-DHyv sequence, the hydrogen bonds are of type I, an apparent exception to the generally observed type II conforma tion for the L D sequence. The ω values for the six amide or ester bonds range from 165° to 172° compared to 180° for planar conformations.
1 X-Ray Analysis 35 becomes fairly extended. The terminal glycine residue has a nonplanar amide bond with an ω value of 159°. A classic parallel pleated sheet structure is exhibited in the crystal by Gly-LPhe-Gly, as shown in Fig. 26 (Marsh and Glusker, 1961), where Ν Η · · O = C hydrogen bonds are formed between the adjacent molecules. The phenylalanine side-chain group is extended away from the polar moieties of the peptide chain. An example of an antiparallel pleated sheet is shown by the iAla-iAla-LAla molecules (Fig.