about
VitAL: Viterbi algorithm for de novo peptide designEntropy Transfer between Residue Pairs and Allostery in Proteins: Quantifying Allosteric Communication in UbiquitinThe elastic net algorithm and protein structure prediction.DNABINDPROT: fluctuation-based predictor of DNA-binding residues within a network of interacting residues.Conformational energies and entropies of peptides, and the peptide-protein binding problem.Computational basis of knowledge-based conformational probabilities derived from local- and long-range interactions in proteins.Predicting important residues and interaction pathways in proteins using Gaussian Network Model: binding and stability of HLA proteins.Prediction of optimal folding routes of proteins that satisfy the principle of lowest entropy loss: dynamic contact maps and optimal controlIdentification of ligand binding sites of proteins using the Gaussian Network Model.Molecular recognition of H3/H4 histone tails by the tudor domains of JMJD2A: a comparative molecular dynamics simulations studyA comparative molecular dynamics study of methylation state specificity of JMJD2A.Predicting most probable conformations of a given peptide sequence in the random coil state.The gaussian network model: precise prediction of residue fluctuations and application to binding problems.Efficient characterization of collective motions and interresidue correlations in proteins by low-resolution simulations.Relationships between amino acid sequence and backbone torsion angle preferences.Turkey must end violent response to protests.The introduction of hydrogen bond and hydrophobicity effects into the rotational isomeric states model for conformational analysis of unfolded peptides.Computational and experimental investigation of DNA repair protein photolyase interactions with low molecular weight drugs.Binding Stability of Peptides on Major Histocompatibility Complex Class I Proteins: Role of Entropy and Dynamics.Relating the Structure of HIV-1 Reverse Transcriptase to Its Processing Step.Collective motions in HIV-1 reverse transcriptase: examination of flexibility and enzyme function.Causality, transfer entropy, and allosteric communication landscapes in proteins with harmonic interactions.Effects of ligand binding upon flexibility of proteins.Conformational transitions in the Ramachandran space of amino acids using the dynamic rotational isomeric state (DRIS) model.Optimum folding pathways of proteins: their determination and properties.Folding dynamics of proteins from denatured to native state: principal component analysis.Determination of pair-wise inter-residue interaction forces from folding pathways and their implementation in coarse-grained folding prediction.Statistical thermodynamics of residue fluctuations in native proteins.Analysis of correlations between energy and residue fluctuations in native proteins and determination of specific sites for binding.Minimum energy configurations of the 2-dimensional HP-model of proteins by self-organizing networks.Eugene GuthMATHEMATICAL MODELING OF BEHÇET'S DISEASE: A DYNAMICAL SYSTEMS APPROACHSimulation of temporal stochastic phenomena in electronic and biological systems: A comparative review, examples and synergiesPrediction of binding sites in receptor-ligand complexes with the Gaussian Network ModelAnharmonicity, mode-coupling and entropy in a fluctuating native proteinQuasi-harmonic analysis of mode coupling in fluctuating native proteinsRelationships between ligand binding sites, protein architecture and correlated paths of energy and conformational fluctuationsQuasi-harmonic fluctuations of two bound peptidesA fast approximate method of identifying paths of allosteric communication in proteinsMode coupling points to functionally important residues in myosin II
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P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Burak Erman
@ast
Burak Erman
@en
Burak Erman
@es
Burak Erman
@nl
type
label
Burak Erman
@ast
Burak Erman
@en
Burak Erman
@es
Burak Erman
@nl
prefLabel
Burak Erman
@ast
Burak Erman
@en
Burak Erman
@es
Burak Erman
@nl
P106
P108
P1153
56243116800
P31
P496
0000-0002-2496-6059