1SB52 A powerful driving force in protein folding
نویسندگان
چکیده
منابع مشابه
Origin of Native Driving Force in Protein Folding
We derive an expression with four adjustable parameters that reproduces well the 20×20 MiyazawaJernigan potential matrix extracted from known protein structures. The numerical values of the parameters can be approximately computed from the surface tension of water, water-screened dipole interactions between residues and water and among residues, and average exposures of residues in folded prote...
متن کاملOrigin of the native driving force for protein folding.
We derive an expression with four adjustable parameters that reproduces well the 20x20 Miyazawa-Jernigan potential matrix extracted from known protein structures. The numerical values of the parameters can be approximately computed from the surface tension of water, water-screened dipole interactions between residues and water and among residues, and average exposures of residues in folded prot...
متن کاملProtein folding as a driving force for dual protein targeting in eukaryotes
It is well documented that in eukaryotic cells molecules of one protein can be located in several subcellular locations, a phenomenon termed dual targeting, dual localization, or dual distribution. The differently localized identical or nearly identical proteins are termed "echoforms." Our conventional definition of dual targeted proteins refers to situations in which one of the echoforms is tr...
متن کاملProtein folding: complex potential for the driving force in a two-dimensional space of collective variables.
Using the Helmholtz decomposition of the vector field of folding fluxes in a two-dimensional space of collective variables, a potential of the driving force for protein folding is introduced. The potential has two components. One component is responsible for the source and sink of the folding flows, which represent respectively, the unfolded states and the native state of the protein, and the o...
متن کاملProtein folding in a force clamp.
Kinetics of folding of a protein held in a force clamp are compared to an unconstrained folding. The comparison is made within a simple topology-based dynamical model of ubiquitin. We demonstrate that the experimentally observed variations in the end-to-end distance reflect microscopic events during folding. However, the folding scenarios in and out of the force clamp are distinct.
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2004
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.44.s9_3