Determining isoleucine side-chain rotamer-sampling in proteins from 13 C chemical shift

Chemical shifts are often the only nuclear magnetic resonance parameter that can be obtained for challenging macromolecular systems. Here we present a framework to derive the conformational sampling of isoleucine side chains from C chemical shifts and demonstrate that side-chain conformations in a l...

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Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2019-12, Vol.55 (94), p.14107-14110
Main Authors: Siemons, Lucas, Uluca-Yazgi, Boran, Pritchard, Ruth B, McCarthy, Stephen, Heise, Henrike, Hansen, D Flemming
Format: Article
Language:English
Subjects:
Carbon Isotopes
Density Functional Theory
Isoleucine - analysis
Isoleucine - chemistry
Nuclear Magnetic Resonance, Biomolecular
Protein Conformation
Proteins - chemistry
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Summary:Chemical shifts are often the only nuclear magnetic resonance parameter that can be obtained for challenging macromolecular systems. Here we present a framework to derive the conformational sampling of isoleucine side chains from C chemical shifts and demonstrate that side-chain conformations in a low-populated folding intermediate can be determined.
ISSN:1359-7345
1364-548X
DOI:10.1039/C9CC06496F