Document Detail


Nuclear-magnetic-resonance studies of eukaryotic cytochrome c. Assignment of resonances of aliphatic amino acids.
MedLine Citation:
PMID:  6244159     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The aliphatic regions of the nuclear magnetic resonance spectra of horse ferricytochrome c and horse ferrocytochrome c are described. Resonance assignments have been made using NMR double-resonance techniques, spectral comparison of related proteins, the perturbing effects of extrinsic probes, and from knowledge of the X-ray structure of cytochrome c. There are eight firmly assigned methyl resonances of ferrocytochrome c and seven firmly assigned methyl resonances of ferricytochrome c.
Authors:
G R Moore; R J Williams
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Publication Detail:
Type:  Comparative Study; Journal Article    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  103     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  1980 Feb 
Date Detail:
Created Date:  1980-05-14     Completed Date:  1980-05-14     Revised Date:  2007-07-23    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  GERMANY, WEST    
Other Details:
Languages:  eng     Pagination:  503-12     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Amino Acids / analysis*
Animals
Cytochrome c Group*
Horses
Magnetic Resonance Spectroscopy
Protein Conformation
Species Specificity
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Cytochrome c Group

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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