Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
THE USE OF PSEUDOCONTACT SHIFTS TO REFINE SOLUTION OF PARAMAGNETIC METALLOPROTEINS - MET80ALA CYANO-CYTOCHROME-C AS AN EXAMPLE
Autore:
BANCI L; BERTINI I; BREN KL; CREMONINI MA; GRAY HB; LUCHINAT C; TURANO P;
Indirizzi:
UNIV FLORENCE,DEPT CHEM,VIA GINO CAPPONI 7 I-50121 FLORENCE ITALY UNIV FLORENCE,DEPT CHEM I-50121 FLORENCE ITALY CALTECH,ARTHUR AMOS NOYES LAB CHEM PHYS PASADENA CA 91125 UNIV BOLOGNA,INST AGR CHEM I-40127 BOLOGNA ITALY
Titolo Testata:
JBIC. Journal of biological inorganic chemistry
fascicolo: 2, volume: 1, anno: 1996,
pagine: 117 - 126
SICI:
0949-8257(1996)1:2<117:TUOPST>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR-MAGNETIC-RESONANCE; 3-DIMENSIONAL SOLUTION STRUCTURE; IRON-SULFUR PROTEIN; HEME ELECTRONIC-STRUCTURE; CHEMICAL-SHIFTS; QUANTITATIVE-DETERMINATION; YEAST ISO-1-CYTOCHROME-C; HORSERADISH-PEROXIDASE; SUSCEPTIBILITY TENSOR; CONFORMATIONAL ENERGY;
Keywords:
SOLUTION STRUCTURE; PARAMAGNETIC BIOMOLECULES; NMR; CYTOCHROME C;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
50
Recensione:
Indirizzi per estratti:
Citazione:
L. Banci et al., "THE USE OF PSEUDOCONTACT SHIFTS TO REFINE SOLUTION OF PARAMAGNETIC METALLOPROTEINS - MET80ALA CYANO-CYTOCHROME-C AS AN EXAMPLE", JBIC. Journal of biological inorganic chemistry, 1(2), 1996, pp. 117-126

Abstract

The availability of NOE constraints and of the relative solution structure of a paramagnetic protein permits the use of pseudocontact shifts as further structural constraints. We have developed a strategy based on: (1) determination of the chi tensor anisotropy parameters from the starting structure; (2) recalculation of a new structure by using NOE and pseudocontact shift constraints simultaneously; (3) redetermination of the chi tensor anisotropy parameters from the new structure, and so on until self-consistency. The system investigated is the cyanide derivative of a variant of the oxidized Saccharomyces cerevisiae iso-1-cytochrome c containing the Met80Ala mutation. The structure has been substantially refined. It is shown that the analysis of the deviation of the experimental pseudocontact shifts from those calculated using the starting structure may be unsound, as may the simple structure refinement based on the pseudocontact shift constraints only.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/07/20 alle ore 22:58:36