Global optimization and folding pathways of selected alpha-helical proteins.
about
The energy landscape, folding pathways and the kinetics of a knotted proteinProtein structure prediction: assembly of secondary structure elements by basin-hopping.Protein structure prediction using basin-hopping.Energy landscapes of a hairpin peptide including NMR chemical shift restraints.Analysis of the Contrasting Pathogenicities Induced by the D222G Mutation in 1918 and 2009 Pandemic Influenza A VirusesProtein structure prediction using global optimization by basin-hopping with NMR shift restraints.Reliable protein folding on complex energy landscapes: the free energy reaction pathEuclidean sections of protein conformation space and their implications in dimensionality reduction.MC EMiNEM maps the interaction landscape of the MediatorUsing an amino acid fluorescence resonance energy transfer pair to probe protein unfolding: application to the villin headpiece subdomain and the LysM domain.Native state conformational heterogeneity of HP35 revealed by time-resolved FRET.Graph representation of protein free energy landscapeProbing the folding transition state structure of the villin headpiece subdomain via side chain and backbone mutagenesis.Observation time scale, free-energy landscapes, and molecular symmetry.The fast-folding HP35 double mutant has a substantially reduced primary folding free energy barrier.The role of binding site on the mechanical unfolding mechanism of ubiquitin.Efficient softest mode finding in transition states calculations.PathOpt--a global transition state search approach: outline of algorithm.Temporal disconnectivity of the energy landscape in glassy systems.Defining and quantifying frustration in the energy landscape: Applications to atomic and molecular clusters, biomolecules, jammed and glassy systems.Multifunctional energy landscape for a DNA G-quadruplex: An evolved molecular switch.Markov state modeling and dynamical coarse-graining via discrete relaxation path sampling.Optimum folding pathways of proteins: their determination and properties.Moving least-squares enhanced Shepard interpolation for the fast marching and string methodsBasin Hopping as a General and Versatile Optimization Framework for the Characterization of Biological Macromolecules
P2860
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P2860
Global optimization and folding pathways of selected alpha-helical proteins.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
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2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh-hant
name
Global optimization and folding pathways of selected alpha-helical proteins.
@en
Global optimization and folding pathways of selected alpha-helical proteins.
@nl
type
label
Global optimization and folding pathways of selected alpha-helical proteins.
@en
Global optimization and folding pathways of selected alpha-helical proteins.
@nl
prefLabel
Global optimization and folding pathways of selected alpha-helical proteins.
@en
Global optimization and folding pathways of selected alpha-helical proteins.
@nl
P2860
P356
P1476
Global optimization and folding pathways of selected alpha-helical proteins.
@en
P2093
David J Wales
Joanne M Carr
P2860
P304
P356
10.1063/1.2135783
P407
P577
2005-12-01T00:00:00Z