Molecular orbital study of polarity and hydrogen bonding effects on thegand hyperfine tensors of site directed NO spin labelled bacteriorhodopsin-Reference-Cited by-同舟云学术

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Molecular orbital study of polarity and hydrogen bonding effects on thegand hyperfine tensors of site directed NO spin labelled bacteriorhodopsin

Published:2002-12-10 Issue:23 Volume:100 Page:3711-3721
ISSN:0026-8976
Container-title:Molecular Physics
language:en
Short-container-title:Molecular Physics

Author:

PLATO MARTIN,STEINHOFF HEINZ-JÜRGEN,WEGENER CHRISTOPH,TÖRRING JENS T.,SAVITSKY ANTON,MÖBIUS KLAUS

Publisher

Informa UK Limited

Subject

Physical and Theoretical Chemistry,Condensed Matter Physics,Molecular Biology,Biophysics

Link

http://www.tandfonline.com/doi/pdf/10.1080/00268970210166246

Reference26 articles.

1. High-field EPR studies of the structure and conformational changes of site-directed spin labeled bacteriorhodopsin

2. High-field EPR-detected shifts of magnetic tensor components of spin label side chains reveal protein conformational changes: The proton entrance channel of bacteriorhodopsin

3. Optimization of parameters for semiempirical methods I. Method

4. g-Values as a Probe of the Local Protein Environment: High-Field EPR of Tyrosyl Radicals in Ribonucleotide Reductase and Photosystem II

5. On the calculation of G tensors of organic radicals

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