Induced dipole calculation with E(3)-equivariant neural networks and multipole field perturbation
10.1021/acs.jctc.5c02167 · doi-reference
A simple, polarizable, rigid, 3-point water model using the direct polarization approximation
10.1021/acs.jctc.5c00603 · doi-reference
A fast, convenient, polarizable electrostatic model for molecular dynamics
10.1021/acs.jctc.3c01171 · doi-reference
A transferrable range-separated force field for water: Combining the power of both physically-motivated models and machine learning techniques
10.1063/5.0128780 · doi-reference
Phosphorylation drives a dynamic switch in serine/arginine-rich proteins
10.1016/j.str.2013.09.014 · doi-reference
The continuous evolution of biomolecular force fields
10.1016/j.str.2025.05.013 · doi-reference
The intrinsic disorder challenge for AlphaFold: A case study of G3BP1 and pathogenic peptide
10.1016/j.isci.2026.115737 · doi-reference
Force field development and simulations of intrinsically disordered proteins
10.1016/j.sbi.2017.10.008 · doi-reference
How well do force fields capture the strength of salt bridges in proteins?
10.7717/peerj.4967 · doi-reference
Characterization of salt bridges to lysines in the protein G B1 domain
10.1021/ja808223p · doi-reference
Signature of mobile hydrogen bonding of lysine side chains from long-range 15N–13C scalar J-couplings and computation
10.1021/ja202219n · doi-reference
Dynamics of lysine side-chain amino groups in a protein studied by heteronuclear 1H–15N NMR spectroscopy
10.1021/ja107847d · doi-reference
Spatial elucidation of motion in proteins by ensemble-based structure calculation using exact NOEs
10.1038/nsmb.2355 · doi-reference
Solution NMR structure and backbone dynamics of the major cold-shock protein (CspA) from Escherichia coli: Evidence for conformational dynamics in the single-stranded RNA-binding site
10.1021/bi980269j · doi-reference
Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase
10.1021/ja9812610 · doi-reference
Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange
10.1021/bi962018l · doi-reference
Rotational diffusion anisotropy of human ubiquitin from 15N NMR relaxation
10.1021/ja00155a020 · doi-reference
Validating the CHARMM36m protein force field with LJ-PME reveals altered hydrogen bonding dynamics under elevated pressures
10.1038/s42004-021-00537-8 · doi-reference
Inclusion of many-body effects in the additive CHARMM protein CMAP potential results in enhanced cooperativity of α-helix and β-hairpin formation
10.1016/j.bpj.2012.07.042 · doi-reference
Conformation of the backbone in unfolded proteins
10.1021/cr040433a · doi-reference
Designing a 20-residue protein
10.1038/nsb798 · doi-reference
What contributions to protein side-chain dynamics are probed by NMR experiments? A molecular dynamics simulation analysis
10.1016/j.jmb.2005.03.001 · doi-reference
CHARMM36 all-atom additive protein force field: Validation based on comparison to NMR data
10.1002/jcc.23354 · doi-reference
Structural dependencies of interresidue scalar coupling (h3) J NC′ and donor (1)H chemical shifts in the hydrogen bonding regions of proteins
10.1021/ja012674v · doi-reference
Correlation between 3h J NC′ and hydrogen bond length in proteins
10.1021/ja9909024 · doi-reference
Direct observation of hydrogen bonds in proteins by interresidue 3h J NC′ scalar couplings
10.1021/ja983945d · doi-reference
Determination of ψ torsion angle restraints from 3 J (Cα, Cα) and 3 J (Cα, HN) coupling constants in proteins
10.1021/ja9928834 · doi-reference
Protein backbone 1H(N)–13Cα and 15N–13Cα residual dipolar and J couplings: New constraints for NMR structure determination
10.1021/ja049049l · doi-reference
Determination of ϕ and χ1 angles in proteins from 13C–13C three-bond J couplings measured by three-dimensional heteronuclear NMR. How planar is the peptide bond?
10.1021/ja970067v · doi-reference
Optimization of the additive CHARMM all-atom protein force field targeting improved sampling of the backbone ϕ, ψ and side-chain χ1 and χ2 dihedral angles
10.1021/ct300400x · doi-reference
Structure and dynamics of the homologous series of alanine peptides: A joint molecular dynamics/NMR study
10.1021/ja0660406 · doi-reference
Contact electron-spin coupling of nuclear magnetic moments
10.1063/1.1729860 · doi-reference
Are current molecular dynamics force fields too helical?
10.1529/biophysj.108.132696 · doi-reference
CHARMM: The biomolecular simulation program
10.1002/jcc.21287 · doi-reference
Algorithms for macromolecular dynamics and constraint dynamics
10.1080/00268977700102571 · doi-reference
Molecular dynamics simulations of water and biomolecules with a Monte Carlo constant pressure algorithm
10.1016/j.cplett.2003.12.039 · doi-reference
Direct-space corrections enable fast and accurate Lorentz–Berthelot combination rule Lennard–Jones lattice summation
10.1021/acs.jctc.5b00726 · doi-reference
Particle mesh Ewald: An N·log(N) method for Ewald sums in large systems
10.1063/1.464397 · doi-reference
Revised 4-point water model for the classical Drude oscillator polarizable force field: SWM4-HLJ
10.1021/acs.jctc.4c00966 · doi-reference
Computationally efficient polarizable md simulations: A simple water model for the classical Drude oscillator polarizable force field
10.1021/acs.jpclett.4c03451 · doi-reference
