Peptide models VII The ending of the right-handed helices in oligopeptides [For-(Ala)n-NH2 for 2 ⩽ n ⩽ 4] and in proteins

Autor:	Michael A. McAllister, András Perczel, Gabor Endredi, Ödön Farkas, Imre G. Csizmadia, Janos Ladik, Pál Császár
Rok vydání:	1995
Předmět:	chemistry.chemical_classification Oligopeptide Right handed Chemistry Stereochemistry Potential energy surface Ab initio Peptide Physical and Theoretical Chemistry Backbone conformation Condensed Matter Physics Biochemistry
Zdroj:	Journal of Molecular Structure: THEOCHEM. 331:5-10
ISSN:	0166-1280
DOI:	10.1016/0166-1280(94)03972-n
Popis:	The right-handed helical conformation (denoted as αL) of a single amino-acid diamide (e.g. HCONHCHCH3CO NH2) is not a minimum energy conformation on the ab initio potential energy surface. Computations performed on oligopeptides [For-(Ala)n NH2, for n ⩽ 4], revealed that the helix-like conformations do exist if the backbone conformation at the carboxyl-end is of δL type; i.e. (αL)n − 1δL. This suggests that according to SCF computations, the isolated helices end in a type I β-turn (αLδL).
Databáze:	OpenAIRE
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