Document Detail

1H NMR studies on bovine cyclophilin: preliminary structural characterization of this specific cyclosporin A binding protein.
MedLine Citation:
PMID:  3542017     Owner:  NLM     Status:  MEDLINE    
High-field 1H NMR spectroscopy has been used to study the conformation of the cytosolic cyclosporin A binding protein cyclophilin. For the drug-free form of cyclophilin, spectral editing methods in conjunction with a pH titration were used to identify all four His residues present in the protein, and two-dimensional COSY and RELAY spectroscopy was used to elucidate the scalar connectivities in the aromatic and upfield methyl regions of the spectrum. From these scalar connectivities, it was possible to distinguish between inter- and intraresidue dipolar interactions within the aromatic and upfield methyl regions of cyclophilin in the NOESY spectrum. The results of this analysis showed extensive interresidue cross-relaxation among and between these latter spectral regions indicative of the proximal relationships of several of these residues and the presence of a hydrophobic core within cyclophilin.
D C Dalgarno; M W Harding; A Lazarides; R E Handschumacher; I M Armitage
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochemistry     Volume:  25     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  1986 Nov 
Date Detail:
Created Date:  1987-02-27     Completed Date:  1987-02-27     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  6778-84     Citation Subset:  IM    
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MeSH Terms
Carrier Proteins* / isolation & purification,  metabolism
Cyclosporins / metabolism
Magnetic Resonance Spectroscopy / methods
Peptidylprolyl Isomerase
Protein Binding
Protein Conformation
Thymus Gland / metabolism
Grant Support
Reg. No./Substance:
0/Carrier Proteins; 0/Cyclosporins; EC Isomerase

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

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