منابع مشابه
Folding of a pressure-denatured model protein.
The noncovalent complex formed by the association of two fragments of chymotrypsin inhibitor-2 is reversibly denatured by pressure in the absence of chemical denaturants. On pressure release, the complex returned to its original conformation through a biphasic reaction, with first-order rate constants of 0.012 and 0.002 s-1, respectively. The slowest phase arises from an interconversion of the ...
متن کاملProtein folding by distributed computing and the denatured state ensemble.
The distributed computing (DC) paradigm in conjunction with the folding@home (FH) client server has been used to study the folding kinetics of small peptides and proteins, giving excellent agreement with experimentally measured folding rates, although pathways sampled in these simulations are not always consistent with the folding mechanism. In this study, we use a coarse-grain model of protein...
متن کاملProtein folding from a highly disordered denatured state: the folding pathway of chymotrypsin inhibitor 2 at atomic resolution.
Previous experimental and theoretical studies have produced high-resolution descriptions of the native and folding transition states of chymotrypsin inhibitor 2 (CI2). In similar fashion, here we use a combination of NMR experiments and molecular dynamics simulations to examine the conformations populated by CI2 in the denatured state. The denatured state is highly unfolded, but there is some r...
متن کاملFolding pathway of a lattice model for protein folding
The folding of a protein-like heteropolymer is studied by direct simulation of a lattice model that folds rapidly to a well-defined “native” structure. The details of each molecular folding event depend on the random initial conformation as well as the random thermal fluctuations of the polymer. By analysing the statistical properties of hundreds of folding events, a classical folding “pathway”...
متن کاملCSAW: a dynamical model of protein folding
CSAW (conditioned self-avoiding walk) is a model of protein folding that combines the features of SAW (self-avoiding walk) and the MonteCarlo method. It simulates the Brownian motion of a chain-molecule in the presence of interactions. We begin with a simple model that takes into account the hydrophobic effect and hydrogen bonding. The results show that the hydrophobic effect alone establishes ...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1999
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.96.14.7888