Cooperativity and modularity in protein folding
نویسندگان
چکیده
منابع مشابه
Cooperativity and modularity in protein folding
A simple statistical mechanical model proposed by Wako and Saitô has explained the aspects of protein folding surprisingly well. This model was systematically applied to multiple proteins by Muñoz and Eaton and has since been referred to as the Wako-Saitô-Muñoz-Eaton (WSME) model. The success of the WSME model in explaining the folding of many proteins has verified the hypothesis that the foldi...
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How does a protein find its native state without a globally exhaustive search? We propose the "HZ" (hydrophobic zipper) hypothesis: hydrophobic contacts act as constraints that bring other contacts into spatial proximity, which then further constrain and zip up the next contacts, etc. In contrast to helix-coil cooperativity, HZ-heteropolymer collapse cooperativity is driven by nonlocal interact...
متن کاملCooperativity and contact order in protein folding.
The effects of cooperativity are studied within Go-Lennard-Jones models of proteins by making the contact interactions dependent on the proximity to the native conformation. The kinetic universality classes are found to remain the same as in the absence of cooperativity. For a fixed native geometry, small changes in the effective contact map may affect the folding times in a chance way, and, to...
متن کاملModeling two-state cooperativity in protein folding.
A protein model with the pairwise interaction energies varying as the local environment changes, i.e., including some kind of collective effect between the contacts, is proposed. Lattice Monte Carlo simulations on the thermodynamical characteristics and free energy profile show a well-defined two-state behavior and cooperativity of folding for such a model. As a comparison, related simulations ...
متن کامل[16] Cooperativity Principles in Protein Folding
Knowledge of the physical driving forces in proteins is essential for understanding their structures and functions. As polymers, proteins have remarkable thermodynamic and kinetic properties. A well-known observation is that the folding and unfolding of many small single-domain proteins, of which chymotrypsin inhibitor 2 is a prime example, appear to involve only two main states—N (native) and ...
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ژورنال
عنوان ژورنال: Biophysics and Physicobiology
سال: 2016
ISSN: 2189-4779
DOI: 10.2142/biophysico.13.0_281