Increased rigidity of eglin c at acidic pH: evidence from NMR spin relaxation and MD simulations.
Biochemistry
; 42(47): 13856-68, 2003 Dec 02.
Article
em En
| MEDLINE
| ID: mdl-14636053
ABSTRACT
To gain physical insights into how proteins respond to changes in pH, the picosecond to nanosecond time scale dynamics of the small serine protease inhibitor eglin c have been studied by NMR spin relaxation experiments and MD simulations under two pH solution conditions, pH 7 and 3. Like many proteins, eglin c is destabilized by a lowering of the pH, although it retains enough stability to maintain its native conformation at pH 3. Backbone (15)N relaxation results show comparable global tumbling times (tau(m)) and model-free order parameters (S(2)) under the two pH conditions, indicating that the molecule maintains its overall molecular shape and structure at low pH, although the backbone rigidity is slightly increased (
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Base de dados:
MEDLINE
Assunto principal:
Termodinâmica
/
Simulação por Computador
/
Modelos Moleculares
/
Serpinas
Tipo de estudo:
Prognostic_studies
/
Qualitative_research
Limite:
Animals
Idioma:
En
Revista:
Biochemistry
Ano de publicação:
2003
Tipo de documento:
Article
País de afiliação:
Estados Unidos