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Titolo:
SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF THE DELTA-SUBUNIT OF THE ESCHERICHIA-COLI ATPSYNTHASE
Autore:
WILKENS S; DUNN SD; CHANDLER J; DAHLQUIST FW; CAPALDI RA;
Indirizzi:
UNIV OREGON,INST MOL BIOL EUGENE OR 97403 UNIV OREGON,INST MOL BIOL EUGENE OR 97403 UNIV WESTERN ONTARIO,DEPT BIOCHEM LONDON ON N6A 5C1 CANADA
Titolo Testata:
Nature structural biology
fascicolo: 3, volume: 4, anno: 1997,
pagine: 198 - 201
SICI:
1072-8368(1997)4:3<198:SSOTND>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
CONFERRING PROTEIN OSCP; AMINO-ACID-SEQUENCE; ATP SYNTHASE COMPLEX; ESCHERICHIA-COLI; ADENOSINE-TRIPHOSPHATASE; CRYOELECTRON MICROSCOPY; N-15-LABELED PROTEINS; HEART-MITOCHONDRIA; COUPLING-CONSTANTS; ALPHA-SUBUNIT;
Tipo documento:
Letter
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
40
Recensione:
Indirizzi per estratti:
Citazione:
S. Wilkens et al., "SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF THE DELTA-SUBUNIT OF THE ESCHERICHIA-COLI ATPSYNTHASE", Nature structural biology, 4(3), 1997, pp. 198-201

Abstract

NMR studies of the delta subunit of the Escherichia coli F1F1-ATPsynthase reveal that it consists of an N-terminal six alpha-helix bundle and a less well ordered C terminus. Both domains are part of one of twoseparate connections between F-1 and F-0.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/07/20 alle ore 14:52:54