Exploring the trigger sequence of the GCN4 coiled-coil: Biased molecular dynamics resolves apparent inconsistencies in NMR measurements

scientific article

Exploring the trigger sequence of the GCN4 coiled-coil: Biased molecular dynamics resolves apparent inconsistencies in NMR measurements is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1002/PRO.528
P932PMC publication ID3009413
P698PubMed publication ID20954244
P5875ResearchGate publication ID47451472

P50authorMichel O SteinmetzQ47451321
Wilfred F van GunsterenQ52153822
Jozica DolencQ59002361
P2093author name stringJohn H Missimer
P2860cites workMolecular basis of coiled-coil formationQ27644473
VMD: visual molecular dynamicsQ27860554
Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical featuresQ27860675
The Xplor-NIH NMR molecular structure determination packageQ27860805
Coiled coils: a highly versatile protein folding motifQ29616419
A biomolecular force field based on the free enthalpy of hydration and solvation: the GROMOS force-field parameter sets 53A5 and 53A6Q29617517
Configurational entropy elucidates the role of salt-bridge networks in protein thermostability.Q30362522
Validation of the 53A6 GROMOS force fieldQ30986204
A method to explore protein side chain conformational variability using experimental dataQ33514507
Comparing geometric and kinetic cluster algorithms for molecular simulation dataQ33532746
Methods of NMR structure refinement: molecular dynamics simulations improve the agreement with measured NMR data of a C-terminal peptide of GCN4-p1.Q33594517
The structure of alpha-helical coiled coilsQ34412200
The GROMOS software for biomolecular simulation: GROMOS05.Q34457783
Microdissection of the sequence and structure of intermediate filament chainsQ36101275
Dynamical studies of peptide motifs in the Plasmodium falciparum circumsporozoite surface protein by restrained and unrestrained MD simulationsQ36858279
Calibration of the angular dependence of the amide proton-C alpha proton coupling constants, 3JHN alpha, in a globular protein. Use of 3JHN alpha for identification of helical secondary structureQ39339655
Structure refinement using time-averaged J-coupling constant restraints.Q52404219
Folding-unfolding thermodynamics of a beta-heptapeptide from equilibrium simulationsQ74452346
P433issue12
P921main subjectbiasQ742736
molecular dynamics simulationQ901663
P304page(s)2462-2474
P577publication date2010-12-01
P1433published inProtein ScienceQ7251445
P1476titleExploring the trigger sequence of the GCN4 coiled-coil: biased molecular dynamics resolves apparent inconsistencies in NMR measurements
P478volume19

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cites work (P2860)
Q36373046Assessing and refining molecular dynamics simulations of proteins with nuclear magnetic resonance data.
Q57204634Bestimmung von Strukturinformation aus experimentellen Messdaten für Biomoleküle
Q28484154Biochemical and molecular dynamic simulation analysis of a weak coiled coil association between kinesin-II stalks
Q31143273Deriving Structural Information from Experimentally Measured Data on Biomolecules.
Q37956882Understanding biomolecular motion, recognition, and allostery by use of conformational ensembles.

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