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Protein conformational dynamics and phenotypic switching
(2021-01-01)
Intrinsically disordered proteins (IDPs) are proteins that lack rigid 3D structure but exist as conformational ensembles. Because of their structural plasticity, they can interact with multiple partners. The protein ...
Analyzing the effect of homogeneous frustration in protein folding
(2013-10-01)
The energy landscape theory has been an invaluable theoretical framework in the understanding of biological processes such as protein folding, oligomerization, and functional transitions. According to the theory, the energy ...
Analyzing the effect of homogeneous frustration in protein folding
(2013-10-01)
The energy landscape theory has been an invaluable theoretical framework in the understanding of biological processes such as protein folding, oligomerization, and functional transitions. According to the theory, the energy ...
Unusual dimerization of a BcCsp mutant leads to reduced conformational dynamics
(Wiley, 2017)
Cold shock proteins (Csp) constitute a family of ubiquitous small proteins that act as RNA-chaperones to avoid cold-induced termination of translation. All members contain two subdomains composed of 2 and 3 beta-strands, ...
On the analysis and comparison of conformer-specific essential dynamics upon ligand binding to a protein
(American Institute of Physics, 2015-06)
The native state of a protein consists of an equilibrium of conformational states on an energy landscape rather than existing as a single static state. The co-existence of conformers with different ligand-affinities in a ...
Collective variable driven molecular dynamics to improve protein protein docking scoring
(Elsevier, 2013-12-28)
In biophysics, the structural prediction of protein–protein complexes starting from the unbound form of the two interacting monomers is a major difficulty. Although current computational docking protocols are able to ...