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

Wenbo Li, Ann E. McDermott

Research output: Contribution to journalArticle

Abstract

New methods for probing dynamical properties of biological macromolecules on the millisecond timescale will enable a better understanding of the structure-function 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.

Original languageEnglish (US)
Pages (from-to)14-22
Number of pages9
JournalConcepts in Magnetic Resonance Part A: Bridging Education and Research
Volume42 A
Issue number1
DOIs
StatePublished - Jan 1 2013
Externally publishedYes

Keywords

  • 2D exchange experiment
  • H decoupling
  • L-phenylalanine hydrochloride
  • Line-shape simulation
  • Millisecond dynamics
  • R-CODEX
  • Solid-state NMR

ASJC Scopus subject areas

  • Spectroscopy

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