Lattice model for rapidly folding protein-like heteropolymers.
AUTOR(ES)
Shrivastava, I
RESUMO
Protein folding is a relatively fast process considering the astronomical number of conformations in which a protein could find itself. Within the framework of a lattice model, we show that one can design rapidly folding sequences by assigning the strongest attractive couplings to the contacts present in a target native state. Our protein design can be extended to situations with both attractive and repulsive contacts. Frustration is minimized by ensuring that all the native contacts are again strongly attractive. Strikingly, this ensures the inevitability of folding and accelerates the folding process by an order of magnitude. The evolutionary implications of our findings are discussed.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=40953Documentos Relacionados
- Statistical mechanics of protein-like heteropolymers
- On constructing folding heteropolymers.
- DNA binding specificity and sequence of Xanthomonas campestris catabolite gene activator protein-like protein.
- Functional Role of Neuroendocrine-Specific Protein-Like 1 in Membrane Translocation of GLUT4
- TATA-Binding Protein-Like Protein (TLP/TRF2/TLF) Negatively Regulates Cell Cycle Progression and Is Required for the Stress-Mediated G2 Checkpoint