Finite size effects on thermal denaturation of globular proteins
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Finite size effects on thermal denaturation of globular proteins
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| Id. |
20880366 |
| Titulo |
Finite size effects on thermal denaturation of globular proteins |
| Autor(es) |
Li, Mai Suan
Klimov, D. K.
Thirumalai, D.
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| Localización |
http://arxiv.org/abs/q-bio/0411050
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| Versión |
1.0 |
| Estado |
Final
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| Descripción |
Finite size effects on the cooperative thermal denaturation of proteins are
considered. A dimensionless measure of cooperativity, Omega, scales as N^zeta,
where N is the number of amino acids. Surprisingly, we find that zeta is
universal with zeta = 1 + gamma, where the exponent gamma characterizes the
divergence of the susceptibility for a self-avoiding walk. Our lattice model
simulations and experimental data are consistent with the theory. Our finding
rationalizes the marginal stability of proteins and substantiates the earlier
predictions that the efficient folding of two-state proteins requires the
folding transition temperature to be close to the collapse temperature.
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| Palabras clave |
Quantitative Biology - Biomolecules
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| Tipo de recurso |
Texto Narrativo
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| Tipo de Interactividad |
Expositivo
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| Nivel de Interactividad |
muy bajo
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| Audiencia |
Estudiante
Profesor
Autor
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| Estructura |
Atomic |
| Coste |
no
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| Copyright |
sí
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| Requerimientos técnicos |
Browser: Any
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| Fecha de contribución |
28-mar-2007 |
| Contacto |
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