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Residual dipolar couplings in short peptidic foldamers: combined analyses of backbone and side-chain conformations and evaluation of structure coordinates of rigid unnatural amino acids

Schmid, Markus B, Fleischmann, Matthias, D'Elia, Valerio, Reiser, Oliver, Gronwald, Wolfram and Gschwind, Ruth M. (2009) Residual dipolar couplings 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:February 2009
Institutions:Medicine > Institut für Funktionelle Genomik > Lehrstuhl für Funktionelle Genomik (Prof. Oefner)
Identification Number:
ValueType
19156789PubMed ID
10.1002/cbic.200800736DOI
Classification:
NotationType
Amino Acids/chemistryMESH
Molecular ConformationMESH
Molecular StructureMESH
Nuclear Magnetic Resonance, BiomolecularMESH
Peptides/chemistryMESH
Protein FoldingMESH
Dewey Decimal Classification:500 Science > 540 Chemistry & allied sciences
500 Science > 570 Life sciences
600 Technology > 610 Medical sciences Medicine
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Partially
Item ID:30655
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