Equilibrium fluctuations of a single folded protein reveal a multitude of potential cryptic allosteric sites. - Wikidata - wikimedia - TriplyDB

Equilibrium fluctuations of a single folded protein reveal a multitude of potential cryptic allosteric sites.

Equilibrium fluctuations of a single folded protein reveal a multitude of potential cryptic allosteric sites.

http://www.wikidata.org/entity/Q34323850

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Principles and Overview of Sampling Methods for Modeling Macromolecular Structure and Dynamics Small Molecule Targeting of Protein-Protein Interactions through Allosteric Modulation of Dynamics Markov state models of biomolecular conformational dynamics Markov state models provide insights into dynamic modulation of protein function The biology of boundary conditions: cellular reconstitution in one, two, and three dimensions Two polymorphisms facilitate differences in plasticity between two chicken major histocompatibility complex class I proteins Selector function of MHC I molecules is determined by protein plasticity Using Markov state models to study self-assembly Quantitative comparison of alternative methods for coarse-graining biological networks Emerging Computational Methods for the Rational Discovery of Allosteric Drugs.Detection of secondary binding sites in proteins using fragment screening Ultra-High-Throughput Structure-Based Virtual Screening for Small-Molecule Inhibitors of Protein-Protein Interactions.Predicting Protein Dynamics and Allostery Using Multi-Protein Atomic Distance Constraints.Extensive conformational heterogeneity within protein cores.Oxygen Pathways and Allostery in Monomeric Sarcosine Oxidase via Single-Sweep Free-Energy Reconstruction Kinetics of protein-ligand unbinding: Predicting pathways, rates, and rate-limiting steps.Mapping the structural and dynamical features of multiple p53 DNA binding domains: insights into loop 1 intrinsic dynamics.Discovery of multiple hidden allosteric sites by combining Markov state models and experiments Insight derived from molecular dynamics simulations into molecular motions, thermodynamics and kinetics of HIV-1 gp120 Molecular dynamics study of naturally existing cavity couplings in proteins.One Crystal, Two Temperatures: Cryocooling Penalties Alter Ligand Binding to Transient Protein Sites.Free energy landscape of activation in a signalling protein at atomic resolution.Conformational Sampling and Binding Site Assessment of Suppression of Tumorigenicity 2 Ectodomain Investigating Dynamic Interdomain Allostery in Pin1 Computational Tools for Allosteric Drug Discovery: Site Identification and Focus Library Design.AIM for Allostery: Using the Ising Model to Understand Information Processing and Transmission in Allosteric Biomolecular Systems.Designing small molecules to target cryptic pockets yields both positive and negative allosteric modulators.HIV-1 Protease Dimerization Dynamics Reveals a Transient Druggable Binding Pocket at the Interface.Markov state models of protein misfolding CryptoSite: Expanding the Druggable Proteome by Characterization and Prediction of Cryptic Binding Sites.Mono and dual cofactor dependence of human cystathionine β-synthase enzyme variants in vivo and in vitro.The Allostery Landscape: Quantifying Thermodynamic Couplings in Biomolecular Systems.Cloud-based simulations on Google Exacycle reveal ligand modulation of GPCR activation pathways.Mapping polymerization and allostery of hemoglobin S using point mutations.Understanding the challenges of protein flexibility in drug design.Exploiting computationally derived out-of-the-box protein conformations for drug design.Systematic Targeting of Protein-Protein Interactions Communication: Consistent interpretation of molecular simulation kinetics using Markov state models biased with external information.Estimation and uncertainty of reversible Markov models.Protein conformational plasticity and complex ligand-binding kinetics explored by atomistic simulations and Markov models.

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P2860

Equilibrium fluctuations of a single folded protein reveal a multitude of potential cryptic allosteric sites.

http://www.wikidata.org/entity/Q34323850

description

2012 nî lūn-bûn

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2012 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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Equilibrium fluctuations of a ...... tial cryptic allosteric sites.

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Equilibrium fluctuations of a ...... tial cryptic allosteric sites.

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Equilibrium fluctuations of a ...... tial cryptic allosteric sites.

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PNAS.1209309109

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

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Gregory R Bowman

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Phillip L Geissler

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P2860

Exploiting a natural conformational switch to engineer an interleukin-2 'superkine'

Markov state model reveals folding and functional dynamics in ultra-long MD trajectories

Novel allosteric sites on Ras for lead generation

Modeling conformational ensembles of slow functional motions in Pin1-WW

Site-directed ligand discovery

Evolution of an antibiotic resistance enzyme constrained by stability and activity trade-offs

Binding of small molecules to an adaptive protein-protein interface

Molecular structure of the acyl-enzyme intermediate in beta-lactam hydrolysis at 1.7 A resolution

Exploitation of structural and regulatory diversity in glutamate racemases

Enzyme adaptation to inhibitor binding: a cryptic binding site in phenylethanolamine N-methyltransferase

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protein folding

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