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

ABSTRACT: 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 13C chemical shifts and demonstrate that side-chain conformations in a low-populated folding intermediate can be determined.

SUBMITTER: Siemons L 

PROVIDER: S-EPMC7138115 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature

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Determining isoleucine side-chain rotamer-sampling in proteins from <sup>13</sup>C chemical shift.

Siemons Lucas L   Uluca-Yazgi Boran B   Pritchard Ruth B RB   McCarthy Stephen S   Heise Henrike H   Hansen D Flemming DF  

Chemical communications (Cambridge, England) 20191023 94

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 <sup>13</sup>C chemical shifts and demonstrate that side-chain conformations in a low-populated folding intermediate can be determined. ...[more]

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