Buscar
Mostrando ítems 1-10 de 433
Protein conformational diversity correlates with evolutionary rate
(Oxford University Press, 2013-04)
Native state of proteins is better represented by an ensemble of conformers in equilibrium than by only one structure. The extension of structural differences between conformers characterizes the conformational diversity ...
Protein conformational diversity modulates sequence divergence
(Oxford University Press, 2012-03)
It is well established that the conservation of protein structure during evolution constrains sequence divergence. The conservation of certain physicochemical environments to preserve protein folds and then the biological ...
CoDNaS: a database of conformational diversity in the native state of proteins
(Oxford University Press, 2013-10)
Motivation: Conformational diversity is a key concept in the understanding of different issues related with protein function such as the study of catalytic processes in enzymes, protein-protein recognition, protein evolution ...
Large scale analysis of protein conformational transitions from aqueous to non-aqueous media
(BioMed Central, 2018-01)
Background: Biocatalysis in organic solvents is nowadays a common practice with a large potential in Biotechnology. Several studies report that proteins which are co-crystallized or soaked in organic solvents preserve their ...
Global conformations of proteins as predicted from the modeling of their CZE mobility data
(Wiley VCH Verlag, 2011-10)
Estimations of protein global conformations in well-specified physicochemical microenvironments are obtained through global structural parameters defined from polypeptide-scale analyses. For this purpose protein electrophoretic ...
The energy cost of polypeptide knot formation and its folding consequences
(Springer Nature, 2017)
Knots are natural topologies of chains. Yet, little is known about spontaneous knot formation in a polypeptide chain-an event that can potentially impair its folding-and about the effect of a knot on the stability and ...
Conformational diversity and the emergence of sequence signatures during evolution
(Current Biology, 2015-03)
Proteins' native structure is an ensemble of conformers in equilibrium, including all their respective functional states and intermediates. The induced-fit first and the pre-equilibrium theories later, described how ...
Renaissance of Allostery to Disrupt Protein Kinase Interactions
(Elsevier Science London, 2019-11)
Protein–protein interactions often regulate the activity of protein kinases by allosterically modulating the conformation of the ATP-binding site. Bidirectional allostery implies that reverse modulation (i.e., from the ...
Evolutionary Conserved Positions Define Protein Conformational Diversity
(Public Library of Science, 2016-03)
Conformational diversity of the native state plays a central role in modulating protein function. The selection paradigm sustains that different ligands shift the conformational equilibrium through their binding to ...
Ultracompact states of native proteins
(Elsevier Science, 2017-11)
A statistical analysis of circa 20,000 X-ray structures evidenced the effects of temperature of data collection on protein intramolecular distances and degree of compaction. Identical chains with data collected at cryogenic ...