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Deconstructing time-resolved optical rotatory dispersion kinetic measurements of cytochrome c folding: from molten globule to the native state.
Chen, Eefei; Kliger, David S.
Afiliação
  • Chen E; Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA, USA. chen@chemistry.ucsc.edu
Methods Mol Biol ; 895: 405-19, 2012.
Article em En | MEDLINE | ID: mdl-22760330
ABSTRACT
The far-UV time-resolved optical rotatory dispersion (TRORD) technique has contributed significantly to our understanding of nanosecond secondary structure kinetics in protein folding and function reactions. For reduced cytochrome c, protein folding kinetics have been probed largely from the unfolded to the native state. Here we provide details about sample preparation and the TRORD apparatus and measurements for studying folding from a partly unfolded state to the native secondary structure conformation of reduced cytochrome c.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Dobramento de Proteína / Citocromos c Idioma: En Revista: Methods Mol Biol Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2012 Tipo de documento: Article País de afiliação: Estados Unidos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Dobramento de Proteína / Citocromos c Idioma: En Revista: Methods Mol Biol Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2012 Tipo de documento: Article País de afiliação: Estados Unidos