Protein folded states are kinetic hubs. - Test2 - elhamkhani - TriplyDB

Protein folded states are kinetic hubs.

Protein folded states are kinetic hubs.

http://www.wikidata.org/entity/Q33934376

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Taming the complexity of protein folding Intrinsically disordered proteins in a physics-based world Markov state model reveals folding and functional dynamics in ultra-long MD trajectories The free energy landscape of small molecule unbinding Modeling conformational ensembles of slow functional motions in Pin1-WW Energetically significant networks of coupled interactions within an unfolded protein A molecular interpretation of 2D IR protein folding experiments with Markov state models Slow unfolded-state structuring in Acyl-CoA binding protein folding revealed by simulation and experiment A simple model predicts experimental folding rates and a hub-like topology Direct observation of parallel folding pathways revealed using a symmetric repeat protein system.Retro operation on the Trp-cage miniprotein sequence produces an unstructured molecule capable of folding similar to the original only upon 2,2,2-trifluoroethanol addition.Evolution, energy landscapes and the paradoxes of protein folding.Towards the prediction of order parameters from molecular dynamics simulations in proteins.Data driven Langevin modeling of biomolecular dynamics.Thermal unfolding of barstar and the properties of interfacial water around the unfolded forms.The role of water in protein's behavior: The two dynamical crossovers studied by NMR and FTIR techniques.Using simulations to provide the framework for experimental protein folding studies Thermodynamics of Deca-alanine Folding in Water.Quantifying the Sources of Kinetic Frustration in Folding Simulations of Small Proteins.Extremely slow intramolecular diffusion in unfolded protein L Recent developments in methods for identifying reaction coordinates.Fast single-molecule FRET spectroscopy: theory and experiment Quantitative comparison of villin headpiece subdomain simulations and triplet-triplet energy transfer experiments Taking Ockham's razor to enzyme dynamics and catalysis.Equilibrium fluctuations of a single folded protein reveal a multitude of potential cryptic allosteric sites.On the Application of Molecular-Dynamics Based Markov State Models to Functional Proteins.Kinetic network study of the diversity and temperature dependence of Trp-Cage folding pathways: combining transition path theory with stochastic simulations.Making connections between ultrafast protein folding kinetics and molecular dynamics simulations.QAARM: quasi-anharmonic autoregressive model reveals molecular recognition pathways in ubiquitin The protein folding network indicates that the ultrafast folding mutant of villin headpiece subdomain has a deeper folding funnel Microscopic events in β-hairpin folding from alternative unfolded ensembles A smoothly decoupled particle interface: new methods for coupling explicit and implicit solvent Structural disorder of folded proteins: isotope-edited 2D IR spectroscopy and Markov state modeling.Systematically constructing kinetic transition network in polypeptide from top to down: trajectory mapping.Free energy landscape of activation in a signalling protein at atomic resolution.Protein folding is mechanistically robust.The role of atomic level steric effects and attractive forces in protein folding The Role of Packaging Sites in Efficient and Specific Virus Assembly Heat dissipation guides activation in signaling proteins Native state conformational heterogeneity of HP35 revealed by time-resolved FRET.

P2860

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P2860

Protein folded states are kinetic hubs.

http://www.wikidata.org/entity/Q33934376

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2010 nî lūn-bûn

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2010 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2010 թվականի հունիսին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Protein folded states are kinetic hubs.

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Protein folded states are kinetic hubs.

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Protein folded states are kinetic hubs.

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Protein folded states are kinetic hubs.

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Protein folded states are kinetic hubs.

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Protein folded states are kinetic hubs.

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PNAS.1003962107

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

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Protein folded states are kinetic hubs.

@en

P2093

Gregory R Bowman

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

Vijay S Pande

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P2860

The roles of entropy and kinetics in structure prediction

Protein folding funnels: a kinetic approach to the sequence-structure relationship

Nucleation, rapid folding, and globular intrachain regions in proteins

Unfolded-state dynamics and structure of protein L characterized by simulation and experiment

Molecular simulation of ab initio protein folding for a millisecond folder NTL9(1-39)

Simulating oligomerization at experimental concentrations and long timescales: A Markov state model approach

Emergence of Scaling in Random Networks

Collective dynamics of 'small-world' networks

Intermediates in the folding reactions of small proteins

The protein folding problem

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10890-10895

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10.1073/PNAS.1003962107

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24

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107

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20534497

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protein folding

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2890711

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