A gradual disruption of tight side-chain packing: 2D 1H-NMR characterization of acid-induced unfolding of CHABII.
Nat Struct Biol
; 6(2): 129-34, 1999 Feb.
Article
em En
| MEDLINE
| ID: mdl-10048923
ABSTRACT
Little is known about the mechanism of the transition between native proteins and partially folded intermediates. Complete assignments of 2D 1H-NOESY spectra of CHABII at 5 degrees C, pH 6.3, 5.5, 4.6 and 4.0, reveal that lowering of pH results in an extensive but gradual disappearance of NOEs, implying a gradual disruption of tight side-chain packing. Moreover, a tertiary packing core is identified at 5 degrees C and pH 4.0, characterized by persistent long-range NOEs. Thus, we suggest that severe disruption of tight side-chain packing of CHABII can occur at a stage where its secondary structure and tertiary topology remain highly native-like.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas
/
Dobramento de Proteína
Idioma:
En
Revista:
Nat Struct Biol
Ano de publicação:
1999
Tipo de documento:
Article