Structural characterization of a methionine-rich, emulsifying protein from sunflower seed.

Pandya, M J; Sessions, R B; Williams, P B; Dempsey, C E; Tatham, A S; Shewry, P R; Clarke, A R

Pandya, M J; Sessions, R B; Williams, P B; Dempsey, C E; Tatham, A S; Shewry, P R; Clarke, A R.

Afiliación

Pandya MJ; Molecular Recognition Centre, School of Medical Sciences, University of Bristol, United Kingdom. maya@biols.sussex.ac.uk

Proteins ; 38(3): 341-9, 2000 Feb 15.

Article en En | MEDLINE | ID: mdl-10713993

RESUMEN

The 2 S seed storage protein, sunflower albumin 8, contains an unusually high proportion of hydrophobic residues including 16 methionines in a mature protein of 103 amino acids. A structural model, based on the known structure of a related protein, has been constructed as a four-helix bundle cross-linked by four disulphide bonds. This model structure is consistent with data from circular dichroism and nuclear magnetic resonance experiments. Analysis of the model's surface shows the presence of a large hydrophobic face that may be responsible for the highly stable emulsions this protein is known to form with oil/water mixtures.

Asunto(s)

Proteínas de Plantas/química; Albuminas 2S de Plantas; Secuencia de Aminoácidos; Antígenos de Plantas; Dicroismo Circular; Helianthus/química; Espectroscopía de Resonancia Magnética; Espectrometría de Masas; Metionina/química; Modelos Moleculares; Datos de Secuencia Molecular; Proteínas de Plantas/aislamiento & purificación; Estructura Cuaternaria de Proteína; Estructura Secundaria de Proteína; Semillas/química; Alineación de Secuencia; Ultracentrifugación

Buscar en Google

Añadir a Mi BVS

Imprimir

XML

PubMed Links

Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Plantas Idioma: En Revista: Proteins Asunto de la revista: BIOQUIMICA Año: 2000 Tipo del documento: Article País de afiliación: Reino Unido Pais de publicación: Estados Unidos

Buscar en Google

Añadir a Mi BVS

Imprimir

XML

PubMed Links