A rigid disulfide-linked nitroxide side chain simplifies the quantitative analysis of PRE data-Reference-Cited by-同舟云学术

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A rigid disulfide-linked nitroxide side chain simplifies the quantitative analysis of PRE data

Published:2011-09 Issue:1-2 Volume:51 Page:105-114
ISSN:0925-2738
Container-title:Journal of Biomolecular NMR
language:en
Short-container-title:J Biomol NMR

Author:

Fawzi Nicolas L.,Fleissner Mark R.,Anthis Nicholas J.,Kálai Tamás,Hideg Kálmán,Hubbell Wayne L.,Clore G. Marius

Publisher

Springer Science and Business Media LLC

Subject

Spectroscopy,Biochemistry

Link

http://link.springer.com/content/pdf/10.1007/s10858-011-9545-x.pdf

Reference53 articles.

1. Altenbach C, Oh KJ, Trabanino RJ, Hideg K, Hubbell WL (2001) Estimation of inter-residue distances in spin labeled proteins at physiological temperatures: experimental strategies and practical limitations. Biochemistry 40:15471–15482

2. Berliner LJ, Grünwald J, Hankovszky HO, Hideg K (1982) A novel reversible thiol-specific spin label: papain active site labeling and inhibition. Anal Biochem 119:450–455

3. Bermejo GA, Strub MP, Ho C, Tjandra N (2009) Determination of the solution-bound conformation of an amino acid binding protein by NMR paramagnetic relaxation enhancement: use of a single flexible paramagnetic probe with improved estimation of its sampling space. J Am Chem Soc 131:9532–9537

4. Bridges MD, Hideg K, Hubbell WL (2010) Resolving conformational and rotameric exchange in spin-labeled proteins using saturation recovery EPR. Appl Magn Reson 37:363–390

5. Budil DE, Lee S, Saxena S, Freed JH (1996) Nonlinear-least-squares analysis of slow-motion EPR spectra in one and two dimensions using a modified Levenberg-Marquardt algorithm. J Magn Reson Ser A 120:155–189

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