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New structures of allosteric proteins revealing remarkable conformational changes.
Mattevi, A; Rizzi, M; Bolognesi, M.
Afiliación
  • Mattevi A; Department of Genetics & Microbiology, University of Pavia, Italy. mattevi@ipvgen.unipv.it
Curr Opin Struct Biol ; 6(6): 824-9, 1996 Dec.
Article en En | MEDLINE | ID: mdl-8994883
ABSTRACT
New three-dimensional structures of allosteric proteins reveal they have a flexible architecture that is instrumental to the regulation of protein function. Highlights are the structures of GroEL, pyruvate kinase, D-3-phosphoglycerate dehydrogenase and the acetylcholine receptor. Furthermore, significant progress in understanding the nature of the intermediates involved in an allosteric reaction has been achieved through recent spectroscopic and crystallographic studies on haemoglobin.
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Bases de datos: MEDLINE Asunto principal: Proteínas Idioma: En Revista: Curr Opin Struct Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 1996 Tipo del documento: Article País de afiliación: Italia
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Bases de datos: MEDLINE Asunto principal: Proteínas Idioma: En Revista: Curr Opin Struct Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 1996 Tipo del documento: Article País de afiliación: Italia