Coupled folding-binding versus docking: A lattice model study

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Abstract

Using a simple hydrophobic/polar protein model, we perform a Monte Carlo study of the thermodynamics and kinetics of binding to a target structure for two closely related sequences, one of which has a unique folded state while the other is unstructured. We obtain significant differences in their binding behavior. The stable sequence has rigid docking as its preferred binding mode, while the unstructured chain tends to first attach to the target and then fold. The free-energy profiles associated with these two binding modes are compared. (C) 2004 American Institute of Physics.

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Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Biofysik
Originalspråkengelska
Sidor (från-till)3983-3989
TidskriftJournal of Chemical Physics
Volym120
Utgivningsnummer8
StatusPublished - 2004
PublikationskategoriForskning
Peer review utfördJa