about
A universal trend among proteomes indicates an oily last common ancestorAll-atom model for stabilization of alpha-helical structure in peptides by hydrocarbon staples.ELISA: structure-function inferences based on statistically significant and evolutionarily inspired observationsPredicting specificity-determining residues in two large eukaryotic transcription factor familiesEntropic stabilization of proteins and its proteomic consequencesPDB-UF: database of predicted enzymatic functions for unannotated protein structures from structural genomics.Merging molecular mechanism and evolution: theory and computation at the interface of biophysics and evolutionary population geneticsThe interface of protein structure, protein biophysics, and molecular evolutionCombinatorial computational method gives new picomolar ligands for a known enzymeRobustness of atomistic Gō models in predicting native-like folding intermediates.Reconstruction of the src-SH3 protein domain transition state ensemble using multiscale molecular dynamics simulations.Nucleation and the transition state of the SH3 domain.Direct molecular dynamics observation of protein folding transition state ensembleMolecular dynamics simulation of the SH3 domain aggregation suggests a generic amyloidogenesis mechanism.Topological determinants of protein folding.Thermodynamics and folding kinetics analysis of the SH3 domain form discrete molecular dynamics.Different circular permutations produced different folding nuclei in proteins: a computational study.Kinetics, thermodynamics and evolution of non-native interactions in a protein folding nucleus.Statistical significance of protein structure prediction by threading.Side-chain dynamics and protein folding.Imprint of evolution on protein structures.Protein structure and evolutionary history determine sequence space topologyGeometric and physical considerations for realistic protein models.On the origin and highly likely completeness of single-domain protein structures.A structure-centric view of protein evolution, design, and adaptation.The mechanical unfolding of ubiquitin through all-atom Monte Carlo simulation with a Go-type potential.Influenza A H1N1 pandemic strain evolution--divergence and the potential for antigenic drift variants.Improvisation in evolution of genes and genomes: whose structure is it anyway?Benchmarking Inverse Statistical Approaches for Protein Structure and Design with Exactly Solvable Models.Influence of point mutations on protein structure: probability of a neutral mutation.The Role of Evolutionary Selection in the Dynamics of Protein Structure Evolution.[Fluctuating state of the protein globule]Impact of local and non-local interactions on thermodynamics and kinetics of protein folding.A new approach to the design of stable proteins.How to derive a protein folding potential? A new approach to an old problem.Modeling protein folding: the beauty and power of simplicity.Protein structure prediction by threading. Why it works and why it does not.The folding mechanics of a knotted proteinProtein biophysics explains why highly abundant proteins evolve slowlyFolding kinetics of villin 14T, a protein domain with a central beta-sheet and two hydrophobic cores.
P50
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P50
description
researcher ORCID ID = 0000-0002-4769-2265
@en
wetenschapper
@nl
name
Eugene I Shakhnovich
@nl
Eugene I. Shakhnovich
@en
type
label
Eugene I Shakhnovich
@nl
Eugene I. Shakhnovich
@en
altLabel
E I Shakhnovich
@en
E Shakhnovich
@en
E. I. Shakhnovich
@en
E. Shakhnovich
@en
Eugene I Shakhnovich
@en
Eugene Shakhnovich
@en
Shakhnovich
@en
prefLabel
Eugene I Shakhnovich
@nl
Eugene I. Shakhnovich
@en
P31
P496
0000-0002-4769-2265