Ligand concentration regulates the pathways of coupled protein folding and binding.
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Binding Mechanisms of Intrinsically Disordered Proteins: Theory, Simulation, and ExperimentHow to Distinguish Conformational Selection and Induced Fit Based on Chemical Relaxation RatesMg2+Shifts Ligand-Mediated Folding of a Riboswitch from Induced-Fit to Conformational SelectionType 1 and Type 2 scenarios in hydrogen exchange mass spectrometry studies on protein-ligand complexes.Both protein dynamics and ligand concentration can shift the binding mechanism between conformational selection and induced fitStructural disorder of folded proteins: isotope-edited 2D IR spectroscopy and Markov state modeling.Conformational kinetics reveals affinities of protein conformational states.Electrostatic Energetics of Bacillus subtilis Ribonuclease P Protein Determined by Nuclear Magnetic Resonance-Based Histidine pKa Measurements.A dynamic look backward and forward.What Mutagenesis Can and Cannot Reveal About Allostery.Effects of hesperidin, a flavanone glycoside interaction on the conformation, stability, and aggregation of lysozyme: multispectroscopic and molecular dynamic simulation studies?An integrated perspective on RNA aptamer ligand-recognition models: clearing muddy waters.Rate Constants and Mechanisms of Protein-Ligand Binding.Effects of 2-amino-8-hydroxyquinoline interaction on the conformation of physiological isomers of human serum albumin.RNA Structural Modules Control the Rate and Pathway of RNA Folding and Assembly.Riboswitch structure and dynamics by smFRET microscopyConformational Selection in a Protein-Protein Interaction Revealed by Dynamic Pathway Analysis.Only kinetics can prove conformational selection.Early T cell receptor signals globally modulate ligand:receptor affinities during antigen discrimination.Slow molecular recognition by RNA.A Kinetic Signature for Parallel Pathways: Conformational Selection and Induced Fit. Links and Disconnects between Observed Relaxation Rates and Fractional Equilibrium Flux under Pseudo-First-Order Conditions.Unified understanding of folding and binding mechanisms of globular and intrinsically disordered proteins.pKID Binds to KIX via an Unstructured Transition State with Nonnative Interactions.Flexibility vs Preorganization: Direct Comparison of Binding Kinetics for a Disordered Peptide and Its Exact Preorganized Analogues.Induced Fit Is a Special Case of Conformational Selection.Conserved conformational selection mechanism of Hsp70 chaperone-substrate interactions.Dynamics of the conformational transitions during the dimerization of an intrinsically disordered peptide: a case study on the human islet amyloid polypeptide fragment.
P2860
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P2860
Ligand concentration regulates the pathways of coupled protein folding and binding.
description
2014 nî lūn-bûn
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2014 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Ligand Concentration Regulates the Pathways of Coupled Protein Folding and Binding
@nl
Ligand concentration regulates the pathways of coupled protein folding and binding.
@ast
Ligand concentration regulates the pathways of coupled protein folding and binding.
@en
type
label
Ligand Concentration Regulates the Pathways of Coupled Protein Folding and Binding
@nl
Ligand concentration regulates the pathways of coupled protein folding and binding.
@ast
Ligand concentration regulates the pathways of coupled protein folding and binding.
@en
prefLabel
Ligand Concentration Regulates the Pathways of Coupled Protein Folding and Binding
@nl
Ligand concentration regulates the pathways of coupled protein folding and binding.
@ast
Ligand concentration regulates the pathways of coupled protein folding and binding.
@en
P2093
P2860
P3181
P356
P1476
Ligand concentration regulates the pathways of coupled protein folding and binding
@en
P2093
Carol A Fierke
David R McClure
Kyle G Daniels
Maria A Schumacher
Nam K Tonthat
Scott C Schmidler
Yu-Chu Chang
P2860
P304
P3181
P356
10.1021/JA4086726
P407
P577
2014-01-09T00:00:00Z