Entropy reduction effect imposed by hydrogen bond formation on protein folding cooperativity: evidence from a hydrophobic minimalist model.
Phys Rev E Stat Nonlin Soft Matter Phys
; 72(5 Pt 1): 051903, 2005 Nov.
Article
em En
| MEDLINE
| ID: mdl-16383641
Conformational restrictions imposed by hydrogen bond formation during protein folding are investigated by Monte Carlo simulations of a non-native-centric, two-dimensional, hydrophobic model in which the formation of favorable contacts is coupled to an effective reduction in lattice coordination. This scheme is intended to mimic the requirement that polar backbone groups of real proteins must form hydrogen bonds concomitantly to their burial inside the apolar protein core. In addition to the square lattice, with z=3 conformations per monomer, we use extensions in which diagonal step vectors are allowed, resulting in z=5 and z=7. Thermodynamics are governed by the hydrophobic energy function, according to which hydrophobic monomers tend to make contacts unspecifically while the reverse is true for hydrophilic monomers, with the additional restriction that only contacts between monomers adopting one of zh
Assuntos
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas
/
Modelos Moleculares
/
Análise de Sequência de Proteína
/
Modelos Químicos
Idioma:
En
Revista:
Phys Rev E Stat Nonlin Soft Matter Phys
Assunto da revista:
BIOFISICA
/
FISIOLOGIA
Ano de publicação:
2005
Tipo de documento:
Article
País de afiliação:
Brasil
País de publicação:
Estados Unidos
Buscar no Google
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas
/
Modelos Moleculares
/
Análise de Sequência de Proteína
/
Modelos Químicos
Idioma:
En
Revista:
Phys Rev E Stat Nonlin Soft Matter Phys
Assunto da revista:
BIOFISICA
/
FISIOLOGIA
Ano de publicação:
2005
Tipo de documento:
Article
País de afiliação:
Brasil
País de publicação:
Estados Unidos