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 language | English (US) |
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Pages (from-to) | 14-22 |
Number of pages | 9 |
Journal | Concepts in Magnetic Resonance Part A: Bridging Education and Research |
Volume | 42 A |
Issue number | 1 |
DOIs | |
State | Published - Jan 2013 |
Externally published | Yes |
Keywords
- 2D exchange experiment
- H decoupling
- L-phenylalanine hydrochloride
- Line-shape simulation
- Millisecond dynamics
- R-CODEX
- Solid-state NMR
ASJC Scopus subject areas
- Spectroscopy