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Conformational Preferences in Small Peptide Models: The Relevance of cis/trans-Conformations

Jangra, H., Haindl, M. H., Achrainer, F,, Hioe, J., Gschwind, Ruth Maria and Zipse, H. (2016) Conformational Preferences in Small Peptide Models: The Relevance of cis/trans-Conformations. Chemistry – A European Journal 22 (37), pp. 13328-13335.

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Other URL: http://dx.doi.org/10.1002/chem.201601828


Abstract

The accurate description of cis/trans peptide structures is of fundamental relevance for the field of protein modeling and protein structure determination. A comprehensive conformational analysis of dipeptide model Ace-Gly-NMe (1) has been carried out by using a combination of theoretical calculations and experimental (1H and 13C NMR and NOESY) spectroscopic measurements to assess the relevance ...

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Item type:Article
Date:2016
Institutions:Chemistry and Pharmacy > Institut für Organische Chemie > Arbeitskreis Prof. Dr. Ruth Gschwind
Identification Number:
ValueType
10.1002/chem.201601828DOI
Keywords:conformation analysis, density functional calculations, peptides, protein folding, protein structures
Dewey Decimal Classification:500 Science > 540 Chemistry & allied sciences
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Item ID:35397
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