Validity of Gō models: comparison with a solvent-shielded empirical energy decomposition.
about
Knotted proteins: A tangled tale of Structural BiologyContinuum molecular simulation of large conformational changes during ion-channel gatingSelf-consistent determination of the transition state for protein folding: application to a fibronectin type III domain.Robustness of atomistic Gō models in predicting native-like folding intermediates.The effects of nonnative interactions on protein folding rates: theory and simulationCalculation of mutational free energy changes in transition states for protein folding.Robotically assisted titration coupled to ion mobility-mass spectrometry reveals the interface structures and analysis parameters critical for multiprotein topology mappingMultidimensional persistence in biomolecular dataAnalysis of the free-energy surface of proteins from reversible folding simulations.Nonnative interactions in coupled folding and binding processes of intrinsically disordered proteins.Structural comparison of the two alternative transition states for folding of TI I27.Macromolecular crowding induces polypeptide compaction and decreases folding cooperativityAnalysis of the distributed computing approach applied to the folding of a small beta peptide.Insights from coarse-grained Gō models for protein folding and dynamics.Topological transformations in proteins: effects of heating and proximity of an interface.Specificity of intramembrane protein-lipid interactions.The role of non-native interactions in the folding of knotted proteins: insights from molecular dynamics simulationsImprovement of structure-based potentials for protein folding by native and nonnative hydrogen bonds.Is there an en route folding intermediate for Cold shock proteins?Selection of optimal variants of Gō-like models of proteins through studies of stretchingThe low populated folding intermediate of a mutant of the Fyn SH3 domain identified by a simple model.Dual binding mode in cohesin-dockerin complexes as assessed through stretching studies.Molecular simulation of surfactant-assisted protein refolding.Free energy for protein folding from nonequilibrium simulations using the Jarzynski equality.Thermodynamics of Go-type models for protein folding.New dynamical window onto the landscape for forced protein unfolding.Criteria for folding in structure-based models of proteins.Scaling approach to the folding kinetics of large proteins.
P2860
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P2860
Validity of Gō models: comparison with a solvent-shielded empirical energy decomposition.
description
2002 nî lūn-bûn
@nan
2002 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի դեկտեմբերին հրատարակված գիտական հոդված
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2002年の論文
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2002年論文
@yue
2002年論文
@zh-hant
2002年論文
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2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
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name
Validity of Gō models: comparison with a solvent-shielded empirical energy decomposition
@nl
Validity of Gō models: comparison with a solvent-shielded empirical energy decomposition.
@ast
Validity of Gō models: comparison with a solvent-shielded empirical energy decomposition.
@en
Validity of Gō models: comparison with a solvent-shielded empirical energy decomposition.
@en-gb
type
label
Validity of Gō models: comparison with a solvent-shielded empirical energy decomposition
@nl
Validity of Gō models: comparison with a solvent-shielded empirical energy decomposition.
@ast
Validity of Gō models: comparison with a solvent-shielded empirical energy decomposition.
@en
Validity of Gō models: comparison with a solvent-shielded empirical energy decomposition.
@en-gb
prefLabel
Validity of Gō models: comparison with a solvent-shielded empirical energy decomposition
@nl
Validity of Gō models: comparison with a solvent-shielded empirical energy decomposition.
@ast
Validity of Gō models: comparison with a solvent-shielded empirical energy decomposition.
@en
Validity of Gō models: comparison with a solvent-shielded empirical energy decomposition.
@en-gb
P2860
P50
P1433
P1476
Validity of Gō models: comparison with a solvent-shielded empirical energy decomposition.
@en
P2860
P304
P356
10.1016/S0006-3495(02)75308-3
P407
P577
2002-12-01T00:00:00Z