scholarly article | Q13442814 |
P356 | DOI | 10.1080/08927022.2012.705432 |
P50 | author | Yuko Okamoto | Q51921025 |
P2093 | author name string | Yoshitake Sakae | |
P2860 | cites work | Secondary-structure preferences of force fields for proteins evaluated by generalized-ensemble simulations | Q57906137 |
Optimization of protein force-field parameters with the Protein Data Bank | Q57906159 | ||
Canonical dynamics: Equilibrium phase-space distributions | Q21709091 | ||
Optimization by Simulated Annealing | Q25939004 | ||
All-atom empirical potential for molecular modeling and dynamics studies of proteins | Q27860468 | ||
Comparison of multiple Amber force fields and development of improved protein backbone parameters | Q27861040 | ||
A short linear peptide that folds into a native stable beta-hairpin in aqueous solution | Q28295200 | ||
All-Atom Structure Prediction and Folding Simulations of a Stable Protein | Q29305923 | ||
Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations | Q29547631 | ||
A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations | Q29547632 | ||
Conformation of Polypeptides and Proteins | Q29617878 | ||
Alpha-helical stabilization by side chain shielding of backbone hydrogen bonds | Q34014321 | ||
Generalized-ensemble algorithms for molecular simulations of biopolymers | Q34309528 | ||
Complement assembly of two fragments of the streptococcal protein G B1 domain in aqueous solution | Q36708673 | ||
Nature of the charged-group effect on the stability of the C-peptide helix | Q37684326 | ||
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 solvents | Q44486720 | ||
Improved treatment of the protein backbone in empirical force fields. | Q44735024 | ||
Replica-exchange molecular dynamics method for protein folding | Q55879366 | ||
A Second Generation Force Field for the Simulation of Proteins, Nucleic Acids, and Organic Molecules | Q55918670 | ||
Semianalytical treatment of solvation for molecular mechanics and dynamics | Q56866446 | ||
Controlling the secondary-structure-forming tendencies of proteins by a backbone torsion-energy term | Q57905888 | ||
Secondary-Structure Design of Proteins by a Backbone Torsion Energy | Q57906009 | ||
Comparisons of force fields for proteins by generalized-ensemble simulations | Q57906065 | ||
PROTEIN FORCE-FIELD PARAMETERS OPTIMIZED WITH THE PROTEIN DATA BANK I: FORCE-FIELD OPTIMIZATIONS | Q57906122 | ||
PROTEIN FORCE-FIELD PARAMETERS OPTIMIZED WITH THE PROTEIN DATA BANK II: COMPARISONS OF FORCE FIELDS BY FOLDING SIMULATIONS OF SHORT PEPTIDES | Q57906128 | ||
P433 | issue | 2 | |
P921 | main subject | force field | Q1341441 |
P304 | page(s) | 85-93 | |
P577 | publication date | 2013-02-01 | |
P1433 | published in | Molecular Simulation | Q3319474 |
P1476 | title | Improvement of the backbone-torsion-energy term in the force field for protein systems by the double Fourier series expansion | |
P478 | volume | 39 |
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