Assignment of hyperfine-shifted resonances in yeast ferricytochrome isozyme 2 using the proton pre-steady-state nuclear Overhauser effect
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference31 articles.
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4. Proton magnetic resonance studies of cytochrome c peroxidase: pD dependence of the isotropically shifted resonances
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1. Microsecond structural fluctuations in denatured cytochrome c and the mechanism of rapid chain contraction;Journal of Physics: Condensed Matter;2003-04-28
2. Proton NMR Assignments and Magnetic Axes Orientations for Wild-Type Yeast Iso-1-ferricytochrome c Free in Solution and Bound to Cytochrome c Peroxidase;Biochemistry;1997-04-01
3. Sequential main-chain proton and carbon resonance assignments for wild-type yeast iso-1 ferrocytochrome c and identification of secondary structural elements;Journal of Protein Chemistry;1997
4. A comparison of spectral and physicochemical properties of yeast iso-1 cytochrome c and Cys 102-modified derivatives of the protein;Journal of Protein Chemistry;1995-10
5. Cytochrome c peroxidase-catalyzed oxidation of yeast iso-1 ferrocytochrome c by hydrogen peroxide. Ionic strength dependence of the steady-state parameters;Biochemistry;1995-08-08
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