Improved methods for structural studies of proteins using nuclear magnetic resonance spectroscopy.

Clowes, R T; Crawford, A; Raine, A R; Smith, B O; Laue, E D

Clowes, R T; Crawford, A; Raine, A R; Smith, B O; Laue, E D.

Afiliación

Clowes RT; Department of Biochemistry, University of Cambridge, UK.

Curr Opin Biotechnol ; 6(1): 81-8, 1995 Feb.

Article en En | MEDLINE | ID: mdl-7894084

RESUMEN

The past few years have seen the development of three- and four-dimensional heteronuclear nuclear magnetic resonance methods. Increased sophistication in labelling strategies, use of pulse-field gradients and the application of these methods at higher magnetic fields has, in combination with improved software, allowed studies of the structure, interactions and dynamics of significantly larger proteins (now up to approximately 270 amino acid residues).

Asunto(s)

Espectroscopía de Resonancia Magnética/métodos; Conformación Proteica; Proteínas/química; Animales; Enzimas/química; Estructura Secundaria de Proteína; Sensibilidad y Especificidad

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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Conformación Proteica / Espectroscopía de Resonancia Magnética / Proteínas Tipo de estudio: Diagnostic_studies Límite: Animals Idioma: En Revista: Curr Opin Biotechnol Asunto de la revista: BIOTECNOLOGIA Año: 1995 Tipo del documento: Article Pais de publicación: Reino Unido

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