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Current applications of 19F NMR to studies of protein structure and dynamics

Published:2012-04 Issue: Volume:62 Page:1-33
ISSN:0079-6565
Container-title:Progress in Nuclear Magnetic Resonance Spectroscopy
language:en
Short-container-title:Progress in Nuclear Magnetic Resonance Spectroscopy

Author:

Kitevski-LeBlanc Julianne L.,Prosser R. Scott

Funder

Natural Sciences and Engineering Research Council of Canada

Publisher

Elsevier BV

Subject

Spectroscopy,Nuclear and High Energy Physics,Biochemistry,Analytical Chemistry

Reference152 articles.

1. Real-time and equilibrium F-19-NMR studies reveal the role of domain–domain interactions in the folding of the chaperone PapD;Bann;Proc. Natl Acad. Sci. USA,2002

2. Observation of sequential steps in the folding of intestinal fatty acid binding protein using a slow folding mutant and F-19 NMR;Li;Proc. Natl Acad. Sci. USA,2007

3. Single proline residues can dictate the oxidative folding pathways of cysteine-rich peptides;Boulègue;J. Mol. Biol.,2006

4. F-19 NMR investigation of F-1-ATPase of Escherichia coli using fluorotryptophan labeling;Lee;J. Biochem.,2000

5. Solution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics;Rozovsky;J. Mol. Biol.,2001

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