Wyniki wyszukiwania

Wyszukiwano:
w słowach kluczowych: protein G

Sortuj według:

Ogranicz wyniki do:

Protein modelling with reduced representation: statistical potentials and protein folding mechanism

100%

Ekonomiuk D., Kielbasinski M., Kolinski A.

Acta Biochimica Polonica

2005

tom 52

nr 4

A high resolution reduced model of proteins is used in Monte Carlo dynamics studies of the folding mechanism of a small globular protein, the B1 immunoglobulin-binding domain of streptococcal protein G. It is shown that in order to reproduce the physics of the folding transition, the united atom based model requires a set of knowledge-based potentials mimicking the short-range conformational propensities and protein-like chain stiffness, a model of directional and cooperative hydrogen bonds, and properly designed knowledge-based potentials of the long-range interactions between the side groups. The folding of the model protein is cooperative and very fast. In a single trajectory, a number of folding/unfolding cycles were observed. Typically, the folding process is initiated by assembly of a native-like structure of the C-terminal hairpin. In the next stage the rest of the four-ribbon β-sheet folds. The slowest step of this pathway is the assembly of the central helix on the scaffold of the β-sheet.