about
Screened nonbonded interactions in native proteins manipulate optimal paths for robust residue communication.Network-based models as tools hinting at nonevident protein functionality.Designing molecular dynamics simulations to shift populations of the conformational states of calmodulin.Consistent picture of the reversible thermal unfolding of hen egg-white lysozyme from experiment and molecular dynamicsAssortative mixing in close-packed spatial networks.MD-TASK: a software suite for analyzing molecular dynamics trajectories.Nanosecond motions in proteins impose bounds on the timescale distributions of local dynamics.Local motifs in proteins combine to generate global functional moves.Protonation states of remote residues affect binding-release dynamics of the ligand but not the conformation of apo ferric binding protein.Perturbation-response scanning reveals ligand entry-exit mechanisms of ferric binding protein.How a vicinal layer of solvent modulates the dynamics of proteins.Surfactant formation efficiency of fluorocarbon-hydrocarbon oligomers in supercritical CO2.Understanding the mode of action of ThDP in benzoylformate decarboxylase.Complete mapping of the morphologies of some linear and graft fluorinated co-oligomers in an aprotic solvent by dissipative particle dynamics.Calmodulin readily switches conformation upon protonating high pKa acidic residues.Mechanisms by Which Salt Concentration Moderates the Dynamics of Human Serum Transferrin.Allosteric Modulation of Human Hsp90α Conformational Dynamics.Increased substrate affinity in the Escherichia coli L28R dihydrofolate reductase mutant causes trimethoprim resistance.Predicting long term cooperativity and specific modulators of receptor interactions in human transferrin from dynamics within a single microstate.How orientational order governs collectivity of folded proteins.In silico mutational studies of Hsp70 disclose sites with distinct functional attributes.Perturbation response scanning specifies key regions in subtilisin serine protease for both function and stability.Computational Methods for Efficient Sampling of Protein Landscapes and Disclosing Allosteric RegionsMODE-TASK: large-scale protein motion toolsMODE-TASK: Large-scale protein motion toolsHybrid Usage of Computational Tools in Drug SynthesisSubtle pH differences trigger single residue motions for moderating conformations of calmodulin
P50
Q30359796-033CC4BC-C284-4022-82FE-8085A49C4120Q30414102-A54A794B-C91D-4623-8AE8-F2BADF3F5645Q30715837-CAF09D76-6FC5-4F53-8197-C9310AEDC868Q33711070-8D0BE3C3-9994-45D7-9B42-53246307ED0DQ33778764-42A848E0-5849-48BA-8215-881AD8BD2F48Q36391139-CBC0DB69-A993-4BBD-A0C5-64756F744FF4Q37373475-49EB76BB-C105-4C3C-A03F-48CA87431EC2Q38027494-AD38D15A-21A7-49BA-8FB8-9FC69DAF06BDQ41735837-2352B494-F38A-455A-A7A8-678880D2D0BBQ41889422-012F732E-8764-4F66-B8C9-109BB220AA59Q42810302-6A4F0C6D-8B65-48DA-B196-9E631ED746D9Q43269177-270D1531-4BA0-428A-8C2B-E4091CCFED27Q43290321-1E152B66-51D8-42F4-8E14-051C7EB2AE68Q46948301-2F0BF9C3-46CB-4C3A-88A2-48C460D28DECQ47718635-A662E5D8-A55B-4BA1-912C-3B3936A2D878Q48232454-8F1CF730-EB83-4002-B9C8-DEA956A7F930Q48520744-E7E21050-5775-49E3-8804-43B021F3CFBFQ50910731-4525486C-CABF-4F16-B78E-620393B2F21DQ51459096-F8C864C8-47BD-4E70-B0F7-1E1EB7A36CA2Q51663923-67E1AE1B-E1A8-43C6-8827-E4A5606DFC8FQ51720267-209B2EFC-779E-429C-9073-1E3C97C4E6C0Q53323308-D0CE27FE-1E40-45DF-B6CD-8763E028D82CQ57179258-1EC3FF81-CAF2-4DD8-A84E-7762508DA411Q58861474-B48E8FB8-4110-4474-903A-91A1E2C9F2FAQ58861478-4742182D-3B4B-4128-8452-A190F8C3EC38Q60459583-8373643A-E908-4F4B-9ACC-3983BFDA3472Q82215228-AA5F6178-1E9D-4B0B-84A7-D5E5F9437498
P50
name
Canan Atilgan
@en
type
label
Canan Atilgan
@en
prefLabel
Canan Atilgan
@en