Hydrophobicity density profiles to predict thermal stability enhancement in proteins.
Protein J
; 25(7-8): 529-35, 2006 Dec.
Article
en En
| MEDLINE
| ID: mdl-17106643
A hydrophobicity density is defined for a protein through its hydrophobicity tensor (similar to the inertia tensor), by using the Eisenberg hydrophobicity scale of the hydrophobic amino acids of a protein. This allows calculation of the radii of the corresponding hydrophobic ellipsoid of a protein and thus subsequently of its hydrophobic density. A hydrophobicity density profile is then obtained by simulating point mutations of each amino acid of a protein either to a high hydrophobicity value or to zero hydrophobicity. It is found that an increase in the hydrophobic density of the protein correlates with an increase of its mid-point transition temperature. From this profile it is possible to determine the amino acids or domain stretches in a protein that are most amenable to mutation in order to increase the thermal stability. The model is tested to predict the thermostabilisation effects of two mutations in a beta-glucanase: M29G and M29F. This model is compared with other hydrophobicity-related profiles described by other authors.
Buscar en Google
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas
/
Modelos Químicos
Tipo de estudio:
Prognostic_studies
/
Risk_factors_studies
Idioma:
En
Revista:
Protein J
Asunto de la revista:
BIOQUIMICA
Año:
2006
Tipo del documento:
Article
País de afiliación:
España
Pais de publicación:
Países Bajos