ISSN:
0006-3525
Keywords:
Chemistry
;
Polymer and Materials Science
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
The conformation of the acyclic biscystine peptide S,S′-bis(Boc-Cys-Ala-OMe) has been studied in the solid state by x-ray diffraction, and in solution by1H- and13C-nmr, ir, and CD methods. The peptide molecule has a twofold rotation symmetry and adopts an intramolecular antiparallel β-sheet structure in the solid state. The two antiparallel extended strands are stabilized by two hydrogen bonds between the Boc CO and Ala NH groups [N⃛O 2.964 (3) Å, O⃛HN 2.11 (3) Å, and NH⃛O angle 162 (3)°]. The disulfide bridge has a right-handed conformation with the torsion angle CβSSCβ = 95.8 (2)°. In solution the presence of a twofold rotation symmetry in the molecule is evident from the1H- and13C-nmr spectra. 1H-nmr studies, using solvent and temperature dependencies of NH chemical shifts, paramagnetic radical induced line broadening, and rate of deuterium-hydrogen exchange effects on NH resonances, suggest that Ala NH is solvent shielded and intramolecularly hydrogen bonded in CDCl3 and in (CD3)2SO. Nuclear Overhauser effects observed between Cys CαH and Ala NH protons and ir studies provide evidence of the occurrence of antiparallel β-sheet structure in these solvents. The CD spectra of the peptide in organic solvents are characteristic of those observed for cystine peptides that have been shown to adopt antiparallel β-sheet structures.
Additional Material:
8 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/bip.360300109
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