Improvement of the backbone-torsion-energy term in the force field for protein systems by the double Fourier series expansion

Improvement of the backbone-torsion-energy term in the force field for protein systems by the double Fourier series expansion is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1080/08927022.2012.705432

P50authorYuko OkamotoQ51921025
P2093author name stringYoshitake Sakae
P2860cites workSecondary-structure preferences of force fields for proteins evaluated by generalized-ensemble simulationsQ57906137
Optimization of protein force-field parameters with the Protein Data BankQ57906159
Canonical dynamics: Equilibrium phase-space distributionsQ21709091
Optimization by Simulated AnnealingQ25939004
All-atom empirical potential for molecular modeling and dynamics studies of proteinsQ27860468
Comparison of multiple Amber force fields and development of improved protein backbone parametersQ27861040
A short linear peptide that folds into a native stable beta-hairpin in aqueous solutionQ28295200
All-Atom Structure Prediction and Folding Simulations of a Stable ProteinQ29305923
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
A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculationsQ29547632
Conformation of Polypeptides and ProteinsQ29617878
Alpha-helical stabilization by side chain shielding of backbone hydrogen bondsQ34014321
Generalized-ensemble algorithms for molecular simulations of biopolymersQ34309528
Complement assembly of two fragments of the streptococcal protein G B1 domain in aqueous solutionQ36708673
Nature of the charged-group effect on the stability of the C-peptide helixQ37684326
1H NMR studies of the solution conformations of an analogue of the C-peptide of ribonuclease A.Q43551567
The SAAP force field. A simple approach to a new all-atom protein force field by using single amino acid potential (SAAP) functions in various solventsQ44486720
Improved treatment of the protein backbone in empirical force fields.Q44735024
Replica-exchange molecular dynamics method for protein foldingQ55879366
A Second Generation Force Field for the Simulation of Proteins, Nucleic Acids, and Organic MoleculesQ55918670
Semianalytical treatment of solvation for molecular mechanics and dynamicsQ56866446
Controlling the secondary-structure-forming tendencies of proteins by a backbone torsion-energy termQ57905888
Secondary-Structure Design of Proteins by a Backbone Torsion EnergyQ57906009
Comparisons of force fields for proteins by generalized-ensemble simulationsQ57906065
PROTEIN FORCE-FIELD PARAMETERS OPTIMIZED WITH THE PROTEIN DATA BANK I: FORCE-FIELD OPTIMIZATIONSQ57906122
PROTEIN FORCE-FIELD PARAMETERS OPTIMIZED WITH THE PROTEIN DATA BANK II: COMPARISONS OF FORCE FIELDS BY FOLDING SIMULATIONS OF SHORT PEPTIDESQ57906128
P433issue2
P921main subjectforce fieldQ1341441
P304page(s)85-93
P577publication date2013-02-01
P1433published inMolecular SimulationQ3319474
P1476titleImprovement of the backbone-torsion-energy term in the force field for protein systems by the double Fourier series expansion
P478volume39

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