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RDCs in Short Peptidic Foldamers: Combined Analyses of Backbone and Side Chain Conformations and Evaluation of Structure Coordinates of Rigid Unnatural Amino Acids

Schmid, M. and Fleischmann, M. and D´Elia, V. and Reiser, O. and Gronwald, W. and Gschwind, R. M. (2009) RDCs in Short Peptidic Foldamers: Combined Analyses of Backbone and Side Chain Conformations and Evaluation of Structure Coordinates of Rigid Unnatural Amino Acids. ChemBioChem 10 (3), pp. 440-444.

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Abstract

A flexible tool for rigid systems. Residual dipolar couplings (RDCs) have proven to be valuable NMR structural parameters that provide insights into the backbone conformations of short linear peptidic foldamers, as illustrated here. This study demonstrates that RDCs at natural abundance can provide essential structural information even in the case of short linear peptides with unnatural amino ...

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Item Type:Article
Date:2009
Institutions:Chemistry and Pharmacy > Institut für Organische Chemie > Arbeitskreis Prof. Dr. Ruth Gschwind
Projects:GRK 760, Graduiertenkolleg Medizinische Chemie
Identification Number:
ValueType
10.1002/cbic.200800736 DOI
Subjects:500 Science > 540 Chemistry & allied sciences
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Owner: Nikola Kastner-Pustet
Deposited On:10 Nov 2009 17:07
Last Modified:10 Nov 2009 17:07
Item ID:10617
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