Detection of slow dynamics by solid-state NMR: Application to L-phenylalanine hydrochloride

被引：1

作者：

Li, Wenbo ^{[1
]}

Mcdermott, Ann E. ^{[1
]}

机构：

[1] Columbia Univ, Dept Chem, New York, NY 10027 USA

来源：

CONCEPTS IN MAGNETIC RESONANCE PART A | 2013年 / 42卷 / 01期

关键词：

L-phenylalanine hydrochloride; solid-state NMR; millisecond dynamics; 2D exchange experiment; line-shape simulation; R-CODEX; 1H decoupling; NUCLEAR-MAGNETIC-RESONANCE; DIMENSIONAL EXCHANGE NMR; ANGLE-SPINNING NMR; ROTATING SOLIDS; RING DYNAMICS; H-2; NMR; MOLECULAR REORIENTATIONS; 2-DIMENSIONAL NMR; ORGANIC-SOLIDS; C-13;

D O I：

10.1002/cmr.a.21254

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

New methods for probing dynamical properties of biological macromolecules on the millisecond timescale will enable a better understanding of the structurefunction relationship. In this article, three solid-state NMR detection methods, line-shape analysis, two-dimensional exchange experiments, and a variant of the center-band only detection of exchange (CODEX) experiment called R-CODEX, are used to characterize a crystalline amino acid that serves as a model for motions in solid proteins, L-phenylalanine hydrochloride. The millisecond ring flip motion of the aromatic ring in L-phenylalanine hydrochloride is characterized in detail for the first time. Limitations of these experiments for processes involving submillisecond timescales are also discussed. (c) 2013 Wiley Periodicals, Inc. Concepts Magn Reson Part A 42A: 1422, 2013.

引用

页码：14 / 22

页数：9

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