Related references
Note: Only part of the references are listed.Modified Potential Functions Result in Enhanced Predictions of a Protein Complex by All-Atom Molecular Dynamics Simulations, Confirming a Stepwise Association Process for Native Protein-Protein Interactions
Zhen-lu Li et al.
JOURNAL OF CHEMICAL THEORY AND COMPUTATION (2019)
CHARMM36m: an improved force field for folded and intrinsically disordered proteins
Jing Huang et al.
NATURE METHODS (2017)
Water Dispersion Interactions Strongly Influence Simulated Structural Properties of Disordered Protein States
Stefano Piana et al.
JOURNAL OF PHYSICAL CHEMISTRY B (2015)
Assessing the potential of atomistic molecular dynamics simulations to probe reversible protein-protein recognition and binding
Luciano A. Abriata et al.
SCIENTIFIC REPORTS (2015)
Balanced Protein-Water Interactions Improve Properties of Disordered Proteins and Non-Specific Protein Association
Robert B. Best et al.
JOURNAL OF CHEMICAL THEORY AND COMPUTATION (2014)
Are Current Atomistic Force Fields Accurate Enough to Study Proteins in Crowded Environments?
Drazen Petrov et al.
PLOS COMPUTATIONAL BIOLOGY (2014)
Atomic-level description of ubiquitin folding
Stefano Piana et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2013)
Noncovalent Dimerization of Ubiquitin
Zhu Liu et al.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2012)
Balance between a and β Structures in Ab Initio Protein Folding
Robert B. Best et al.
JOURNAL OF PHYSICAL CHEMISTRY B (2010)
Improved side-chain torsion potentials for the Amber ff99SB protein force field
Kresten Lindorff-Larsen et al.
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS (2010)
A general purpose model for the condensed phases of water: TIP4P/2005
JLF Abascal et al.
JOURNAL OF CHEMICAL PHYSICS (2005)
Development of an improved four-site water model for biomolecular simulations: TIP4P-Ew
HW Horn et al.
JOURNAL OF CHEMICAL PHYSICS (2004)