Although the conformations of two linked peptide units both with glycyl and alanyl residues have been extensively studied,'-$ no systematic investigation of the energies of conformations of two linked peptide units with side chains beyond the CB atom and a comparison with the available crystallograp
Side chain–backbone hydrogen bonds in peptides containing glutamic acid residues
✍ Scribed by Roger Mayer; Gérard Lancelot; Gérard Spach
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1979
- Tongue
- English
- Weight
- 181 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
✦ Synopsis
Over the last few years x-ray diffraction and nmr investigations have been reported for a variety of natural and synthetic peptides in order to enhance our understanding of the conformation of several amino acid side chains and especially those bearing functional groups such as hydroxyl, sulfhydryl, amide, or carboxylate groups. Only a small amount of data is available for glutamic acid: its crystal structure's2 and that of the complex L-argininehg l ~t a m a t e . ~
We have now synthesized several peptides containing glutamic acid residues and investigated their conformation in dimethylsulfoxide (DMSO) solution by nmr spectroscopy. The results suggest the existence of an intramolecular hydrogen bond between the ionized y-carboxylate group (COO-) of the side chain of the glutamic acid residue and
📜 SIMILAR VOLUMES
A survey of 322 proteins showed that the short polar (SP) side chains of four residues, Thr, Ser, Asp, and Asn, have a very strong tendency to form hydrogen bonds with neighboring backbone amides. Specifically, 32% of Thr, 29% of Ser, 26% of Asp, and 19% of Asn engage in such hydrogen bonds. When an
Using the host-guest technique, tentative scales for the helix-inducing power and the (3-structure-forming potential of various side-chain protected amino acid residues in trifluoroethanol are established mainly by CD measurements. The generally lower tendency for (3-structure formation of the host-