Importance of the peptide backbone description in modeling the selectivity filter in potassium channels.

scientific article

Importance of the peptide backbone description in modeling the selectivity filter in potassium channels. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1016/J.BPJ.2009.02.041
P932PMC publication ID2996537
P698PubMed publication ID19450472
P5875ResearchGate publication ID24435311

P50authorTurgut BaştuğQ73199328
P2093author name stringSerdar Kuyucak
P2860cites workChemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolutionQ22337277
Selectivity in K+ channels is due to topological control of the permeant ion's coordinated stateQ24675280
The predominant role of coordination number in potassium channel selectivityQ24681942
Tuning ion coordination architectures to enable selective partitioningQ24685794
All-atom empirical potential for molecular modeling and dynamics studies of proteinsQ27860468
VMD: visual molecular dynamicsQ27860554
Scalable molecular dynamics with NAMDQ27860718
Comparison of multiple Amber force fields and development of improved protein backbone parametersQ27861040
A gate in the selectivity filter of potassium channelsQ28245693
Crystal structure of a mammalian voltage-dependent Shaker family K+ channelQ28260421
Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulationsQ29547631
Theoretical and computational models of biological ion channelsQ30158013
Exploring peptide energy landscapes: a test of force fields and implicit solvent models.Q30343068
A computational study of ion binding and protonation states in the KcsA potassium channel.Q31812432
Conduction properties of the cloned Shaker K+ channelQ34020048
The ionization state and the conformation of Glu-71 in the KcsA K(+) channelQ34177167
Empirical force fields for biological macromolecules: overview and issues.Q34334583
Control of ion selectivity in potassium channels by electrostatic and dynamic properties of carbonyl ligands.Q34358736
Ion conduction and selectivity in K(+) channelsQ34415730
Simulation approaches to ion channel structure-function relationshipsQ34536695
Ion selectivity in potassium channelsQ34547784
Dynamics of K+ ion conduction through Kv1.2.Q35012348
Molecular restraints in the permeation pathway of ion channelsQ35023843
K+ conduction in the selectivity filter of potassium channels is monitored by the charge distribution along their sequenceQ35121309
Long dynamics simulations of proteins using atomistic force fields and a continuum representation of solvent effects: calculation of structural and dynamic propertiesQ35574706
KcsA: it's a potassium channelQ36436387
Free energy via molecular simulation: applications to chemical and biomolecular systemsQ38648060
Energetics of ion permeation, rejection, binding, and block in gramicidin A from free energy simulationsQ42269231
Importance of the CMAP correction to the CHARMM22 protein force field: dynamics of hen lysozymeQ43203629
Improved treatment of the protein backbone in empirical force fields.Q44735024
Role of fluctuations in a snug-fit mechanism of KcsA channel selectivityQ79927015
P433issue10
P407language of work or nameEnglishQ1860
P1104number of pages7
P304page(s)4006-4012
P577publication date2009-05-01
P1433published inBiophysical JournalQ2032955
P1476titleImportance of the peptide backbone description in modeling the selectivity filter in potassium channels
P478volume96

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cites work (P2860)
Q39127424Biobetters From an Integrated Computational/Experimental Approach.
Q34536403Comparative study of the energetics of ion permeation in Kv1.2 and KcsA potassium channels
Q34973773Computational approaches for designing potent and selective analogs of peptide toxins as novel therapeutics
Q26853268Computational studies of marine toxins targeting ion channels
Q37394938Energetics of Multi-Ion Conduction Pathways in Potassium Ion Channels.
Q30538295High-risk long QT syndrome mutations in the Kv7.1 (KCNQ1) pore disrupt the molecular basis for rapid K(+) permeation
Q35746284Mechanism of Ion Permeation in Mammalian Voltage-Gated Sodium Channels
Q53437310Modeling GPCR active state conformations: the β(2)-adrenergic receptor.
Q33639627Molecular dynamics simulations of membrane proteins
Q34061826Molecular dynamics study of binding of µ-conotoxin GIIIA to the voltage-gated sodium channel Na(v)1.4.
Q30393214Selective complexation of K+ and Na+ in simple polarizable ion-ligating systems
Q34792648Systematic study of binding of μ-conotoxins to the sodium channel NaV1.4.
Q36903655The mechanism of Na⁺/K⁺ selectivity in mammalian voltage-gated sodium channels based on molecular dynamics simulation

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