Proton magnetic resonance observations of hydrogen exchange rates and secondary structure in algal ferredoxin
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference13 articles.
1. Dynamic Aspects of Conformational Changes in Biological Macromolecules;Hvidt,1973
2. Hydrogen Exchange
3. Biologically important isotope hybrid compounds in nmr: 1H Fourier transform nmr at unnatural abundance
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1. Sequence Determination of Reduction Potentials by Cysteinyl Hydrogen Bonds and Peptide Dipoles in [4Fe-4S] Ferredoxins;Biophysical Journal;2001-08
2. Computational studies of redox potentials of electron transfer proteins;Simulation and theory of electrostatic interactions in solution;1999
3. Specific deuteration strategy for enhancing direct nuclear Overhauser effects in high-molecular-weight complexes;Journal of the American Chemical Society;1990-10
4. [2] Deuteration in protein proton magnetic resonance;Methods in Enzymology;1989
5. An analysis of g strain in the EPR of two [2Fe2S] ferredoxins. Evidence for a protein rigidity model;Journal of Magnetic Resonance (1969);1986-10
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