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Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts in horse cytochrome c
Weixia Liu
,
Jon Rumbley
, S. Walter Englander
, A. Joshua Wand
Pharmacy Practice and Pharmaceutical Sciences
Research output
:
Contribution to journal
›
Article
›
peer-review
26
Scopus citations
Overview
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Keyphrases
Cytochrome c (Cyt c)
100%
Side Chain
100%
Heteronuclear
100%
G-tensor
100%
NMR Shifts
100%
Resonance Assignment
100%
Chemical Shift
66%
Oxidized State
66%
Mutant Protein
66%
Escherichia Coli
33%
Redox
33%
Electron Spin
33%
Ligand Field
33%
TOCSY
33%
Redox State
33%
Diamagnetic
33%
Triple Resonance
33%
Minimal Media
33%
Structure Change
33%
Standard Triple
33%
Horse Heart Cytochrome c
33%
Dependent Structure
33%
1H Chemical Shifts
33%
Biochemistry, Genetics and Molecular Biology
Wild Type
100%
Resonance Assignment
100%
Cytochrome C
100%
Mutant Protein
66%
Triple Resonance
33%
Correlation Spectroscopy
33%
Escherichia coli
33%