Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins - sprookjes - yvandenbroek - TriplyDB

Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins

Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins

http://www.wikidata.org/entity/Q24653757

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Many local motions cooperate to produce the adenylate kinase conformational transition Structural and energetic basis of allostery The ensemble nature of allostery RNA mimicry by the fap7 adenylate kinase in ribosome biogenesis Allosteric Inhibition of a Zinc-Sensing Transcriptional Repressor: Insights into the Arsenic Repressor (ArsR) Family Exploring the role of conformational heterogeneity in cis-autoproteolytic activation of ThnT.Interconversion of functional motions between mesophilic and thermophilic adenylate kinases Correlated inter-domain motions in adenylate kinase Hotspot mutations in KIT receptor differentially modulate its allosterically coupled conformational dynamics: impact on activation and drug sensitivity Ligand Docking to Intermediate and Close-To-Bound Conformers Generated by an Elastic Network Model Based Algorithm for Highly Flexible Proteins A hinge migration mechanism unlocks the evolution of green-to-red photoconversion in GFP-like proteins.Mutational Constraints on Local Unfolding Inhibit the Rheological Adaptation of von Willebrand Factor.Mechanism of Iron-Dependent Repressor (IdeR) Activation and DNA Binding: A Molecular Dynamics and Protein Structure Network Study Frustration, specific sequence dependence, and nonlinearity in large-amplitude fluctuations of allosteric proteins.Urea-Dependent Adenylate Kinase Activation following Redistribution of Structural States.Misfolding of vWF to pathologically disordered conformations impacts the severity of von Willebrand disease Investigating homology between proteins using energetic profiles Picosecond-resolved fluorescent probes at functionally distinct tryptophans within a thermophilic alcohol dehydrogenase: relationship of temperature-dependent changes in fluorescence to catalysis.Hydrogen tunneling links protein dynamics to enzyme catalysis Update 1 of: Tunneling and dynamics in enzymatic hydride transfer.Importance of protein dynamics during enzymatic C-H bond cleavage catalysis.Apparent tradeoff of higher activity in MMP-12 for enhanced stability and flexibility in MMP-3.Experimental evolution of adenylate kinase reveals contrasting strategies toward protein thermostability.Functional validation of hydrophobic adaptation to physiological temperature in the small heat shock protein αA-crystallin On the roles of substrate binding and hinge unfolding in conformational changes of adenylate kinase.Allosteric communication across the native and mutated KIT receptor tyrosine kinase.Picosecond-resolved fluorescence studies of substrate and cofactor-binding domain mutants in a thermophilic alcohol dehydrogenase uncover an extended network of communication.Induced fit, conformational selection and independent dynamic segments: an extended view of binding events The Role of Protein-Ligand Contacts in Allosteric Regulation of the Escherichia coli Catabolite Activator Protein In the multi-domain protein adenylate kinase, domain insertion facilitates cooperative folding while accommodating function at domain interfaces.Interplay between allostery and intrinsic disorder in an ensemble Global conformational selection and local induced fit for the recognition between intrinsic disordered p53 and CBP Impaired protein conformational landscapes as revealed in anomalous Arrhenius prefactors Structural and kinetic mapping of side-chain exposure onto the protein energy landscape Dual allosteric activation mechanisms in monomeric human glucokinase.Agonism/antagonism switching in allosteric ensembles.Dissecting protein architecture with communication blocks and communicating segment pairs.The Structure of a Thermophilic Kinase Shapes Fitness upon Random Circular Permutation Structural distributions from single-molecule measurements as a tool for molecular mechanics.Mapping the Dynamics Landscape of Conformational Transitions in Enzyme: The Adenylate Kinase Case.

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P2860

Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins

http://www.wikidata.org/entity/Q24653757

description

2009 nî lūn-bûn

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2009 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2009年の論文

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2009年论文

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Rational modulation of conform ...... ctional adaptation in proteins

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Rational modulation of conform ...... ctional adaptation in proteins

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Rational modulation of conform ...... ctional adaptation in proteins

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Rational modulation of conform ...... ctional adaptation in proteins

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

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Rational modulation of conform ...... ctional adaptation in proteins

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D Wayne Bolen

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Travis P Schrank

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Vincent J Hilser

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P2860

Conformational transitions of adenylate kinase: switching by cracking

Kemp elimination catalysts by computational enzyme design

Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding

Structures of the psychrophilic Alteromonas haloplanctis alpha-amylase give insights into cold adaptation at a molecular level

Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state

Hot spots in cold adaptation: localized increases in conformational flexibility in lactate dehydrogenase A4 orthologs of Antarctic notothenioid fishes

A hierarchy of timescales in protein dynamics is linked to enzyme catalysis

Conformational entropy in molecular recognition by proteins.

Psychrophilic enzymes: hot topics in cold adaptation.

Roles of static and dynamic domains in stability and catalysis of adenylate kinase.

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