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NMR and protein folding: Equilibrium and stopped‐flow studies
Author(s) -
Frieden Carl,
Hoeltzli Sydney D.,
Ropson Ira J.
Publication year - 1993
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560021202
Subject(s) - chemistry , folding (dsp implementation) , protein folding , fluorine 19 nmr , amino acid , amide , nmr spectra database , nuclear magnetic resonance spectroscopy , side chain , deuterium , hydrogen–deuterium exchange , phi value analysis , protein design , protein structure , spectral line , stereochemistry , mass spectrometry , biochemistry , chromatography , organic chemistry , physics , polymer , quantum mechanics , astronomy , electrical engineering , engineering
NMR studies are now unraveling the structure of intermediates of protein folding using hydrogen—deuterium exchange methodologies. These studies provide information about the time dependence of formation of secondary structure. They require the ability to assign specific resonances in the NMR spectra to specific amide protons of a protein followed by experiments involving competition between folding and exchange reactions. Another approach is to use 19 F‐substituted amino acids to follow changes in side‐chain environment upon folding. Current techniques of molecular biology allow assignments of 19 F resonances to specific amino acids by site‐directed mutagenesis. It is possible to follow changes and to analyze results from 19 F spectra in real time using a stopped‐flow device incorporated into the NMR spectrometer.