Stereo-hydrophobic potential and topological properties in the protein folding / "Potencial estéreo-hidrofóbico e propriedades topológicas no enovelamento de proteínas".

AUTOR(ES)

Maria Eulália Pinto Tarragó

DATA DE PUBLICAÇÃO

2003

RESUMO

The understanding of the basic principles of the protein folding process may lead to very important applications. Although all significant aspects of this problem are not yet known, experimental and theoretical results have given important contribution on the subject, as, for instance, about the dominant role of the hydrophobic forces. In order to contribute to the identification of significant ingredients for the folding process, the main goal of this work consists in studying the stereo-hydrophobic potential (that is, the hydrophobic potential and a set of steric specificities) related to the folding process of globular proteins, revealing the importance of the steric constraints and the role of the native structure. A minimalist lattice model was employed for this purpose, and more than forty distinct protein-like chains were studied. These chains were designed based on native structures characterized by topological parameters as contact order, χ, long range order and number φ of crankshaft-like structures. The Monte Carlo simulation results show clearly that the folding process depends strongly on the topological attributes of the native structure: thermodynamical and kinetic behavior for chains designed from native structures, presenting smaller χ and higher φ, are very distinguishable from those with higher χ and lower φ. Additionally it was shown that the steric constraints significantly modify the configurational activity, increasing the general conditions for the globule stability, as well changing drastically the shape of the thermal capacity behavior, as a function of the temperature, in comparison with the corresponding results obtained using the hydrophobic potential only, i.e., without the steric specificities.

ASSUNTO(S)

lattice model propriedades termodinâmicas folding de proteínas potencial estéreo-hidrofóbico geometrical properties protein folding capacidade térmica características geométricas folding time propriedades topológicas thermodynamic properties modelo em rede heat capacity tempo de enovelamento stereo-hydrophobic potential topological properties

Documentos Relacionados

• Efeito da amostragem nas propriedades topológicas de redes complexas
• Topological spins solutions on the torus
• Topological determinants of protein folding
• Generalized Simulated Annealing Parameter Sweeping Applied to the Protein Folding Problem
• Tridimensional reconstruction through stereo vision and occlusion detection