Local conformational fluctuations can modulate the coupling between proton binding and global structural transitions in proteins. - Wikidata - wikimedia - TriplyDB

Local conformational fluctuations can modulate the coupling between proton binding and global structural transitions in proteins.

Local conformational fluctuations can modulate the coupling between proton binding and global structural transitions in proteins.

http://www.wikidata.org/entity/Q33934334

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One-microsecond molecular dynamics simulation of channel gating in a nicotinic receptor homologue Automated identification of functional dynamic contact networks from X-ray crystallography Cooperative transition between open and closed conformations in potassium channels pH-Dependent conformational changes in proteins and their effect on experimental pK(a)s: the case of Nitrophorin 4 NMR characterization of the near native and unfolded states of the PTB domain of Dok1: alternate conformations and residual clusters Toward resolution of ambiguity for the unfolded state.The role of negative selection in protein evolution revealed through the energetics of the native state ensemble.Wiggle-predicting functionally flexible regions from primary sequence Identifying allosteric fluctuation transitions between different protein conformational states as applied to Cyclin Dependent Kinase 2.Structure-based predictive models for allosteric hot spots.A semi-supervised learning approach to predict synthetic genetic interactions by combining functional and topological properties of functional gene network.Correlation of structural stability with functional remodeling of high-density lipoproteins: the importance of being disordered.Instantaneous normal modes as an unforced reaction coordinate for protein conformational transitions A new concept to reveal protein dynamics based on energy dissipation.The mechanism of VWF-mediated platelet GPIbalpha binding.Regulation of catch binding by allosteric transitions.Protein dynamics viewed by hydrogen exchange.On the roles of substrate binding and hinge unfolding in conformational changes of adenylate kinase.Allostery and cooperativity revisited.The two-pathway model of the biological catch-bond as a limit of the allosteric model Acid destabilization of the solution conformation of Bcl-xL does not drive its pH-dependent insertion into membranes Homologous ligands accommodated by discrete conformations of a buried cavity.The N-terminal domain of Bcl-xL reversibly binds membranes in a pH-dependent manner.Functional residues serve a dominant role in mediating the cooperativity of the protein ensemble.Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins.Structure fluctuations and conformational changes in protein binding Rapid calculation of protein pKa values using Rosetta.A host-guest relationship in bone morphogenetic protein receptor-II defines specificity in ligand-receptor recognition.Intracellular pH sensors: design principles and functional significance.Large-scale modulation of thermodynamic protein folding barriers linked to electrostatics Light-activated DNA binding in a designed allosteric protein.A mechanism for localized dynamics-driven affinity regulation of the binding of von Willebrand factor to platelet glycoprotein Ibα.An energetic representation of protein architecture that is independent of primary and secondary structure.Evidence for conformational heterogeneity of fission protein Fis1 from Saccharomyces cerevisiae.Local packing modulates diversity of iron pathways and cooperative behavior in eukaryotic and prokaryotic ferritins.Conformational heterogeneity within the LID domain mediates substrate binding to Escherichia coli adenylate kinase: function follows fluctuations.Emerging roles of Na⁺/H⁺ exchangers in epilepsy and developmental brain disorders.Stochastic level-set variational implicit-solvent approach to solute-solvent interfacial fluctuations.Virus-templated FRET platform for the rational design of ratiometric fluorescent nanosensors.A tetrahedral transition state at the active sites of the 20S proteasome is coupled to opening of the alpha-ring channel.

P2860

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P2860

Local conformational fluctuations can modulate the coupling between proton binding and global structural transitions in proteins.

http://www.wikidata.org/entity/Q33934334

description

2005 nî lūn-bûn

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2005 թուականի Մարտին հրատարակուած գիտական յօդուած

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2005 թվականի մարտին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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Local conformational fluctuati ...... tural transitions in proteins.

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Local conformational fluctuati ...... tural transitions in proteins.

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Local conformational fluctuati ...... tural transitions in proteins.

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Local conformational fluctuati ...... tural transitions in proteins.

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Local conformational fluctuati ...... tural transitions in proteins.

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PNAS.0407499102

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Local conformational fluctuati ...... tural transitions in proteins.

@en

P2093

Bertrand García-Moreno E

http://www.w3.org/2001/XMLSchema#string

Steven T Whitten

http://www.w3.org/2001/XMLSchema#string

Vincent J Hilser

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P2860

Poliovirus cell entry: common structural themes in viral cell entry pathways

Solution structure, dynamics, and thermodynamics of the native state ensemble of the Sem-5 C-terminal SH3 domain

The structure and receptor binding properties of the 1918 influenza hemagglutinin

The crystal structure of staphylococcal nuclease refined at 1.7 A resolution

Structure of influenza haemagglutinin at the pH of membrane fusion

Effective energy function for proteins in solution

Electrostatic contributions to molecular free energies in solution

Single-molecule enzymatic dynamics

pKa's of ionizable groups in proteins: atomic detail from a continuum electrostatic model

Electrostatic Contributions to Molecular Free Energies in Solution

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4282-4287

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scholarly article

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10.1073/PNAS.0407499102

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102

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