Chain reversals in model peptides: studies of cystine-containing cyclic peptides. 3. Conformational free energies of cyclization of tetrapeptides of sequence Ac-Cys-Pro-X-Cys-NHMe
| Autor: | C. M. Falcomer, Y. C. Meinwald, I. Choudhary, S. Talluri, P. J. Milburn, Jon Clardy, H. A. Scheraga |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
chemistry.chemical_classification
Tetrapeptide Stereochemistry Cystine General Chemistry Nuclear magnetic resonance spectroscopy Crystal structure Biochemistry Catalysis Cyclic peptide Dissociation constant chemistry.chemical_compound Colloid and Surface Chemistry chemistry Molecule Peptide sequence |
| Zdroj: | Journal of the American Chemical Society. 114:4036-4042 |
| ISSN: | 1520-5126 0002-7863 |
| DOI: | 10.1021/ja00037a003 |
| Popis: | Six tetrapeptides of amino acid sequence Ac-Cys-Pro-X-Cys-NHMe, where X=Asn, Gly, Ser, Phe, Val, and Aib, respectively, were synthesized, and the molecular structures of the cyclic forms of two of them (with X=Ser and Val, respectively) were determined by X-ray diffraction. These two cyclic peptides were found to adopt a type I β-turn conformation centered at Pro-X. The molecular structures of two of the cyclic peptides (withX=Gly and Ser, respectively) were examined by two-dimensional NMR spectroscopy in aqueous solution |
| Databáze: | OpenAIRE |
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