New protein parameters are reported for the all-atom empirical energy function in the CHARMM
program. The parameter evaluation was based on a self-consistent approach designed …

The dynamics of a folded globular protein (bovine pancreatic trypsin inhibitor) have been
studied by solving the equations of motion for the atoms with an empirical potential energy …

Molecular dynamics simulations are important tools for understanding the physical basis of
the structure and function of biological macromolecules. The early view of proteins as …

CHARMM (Chemistry at HARvard Macromolecular Mechanics) is a highly flexible computer
program which uses empirical energy functions to model macromolecular systems. The …

Molecular dynamics—the science of simulating the motions of a system of particles—applied
to biological macromolecules gives the fluctuations in the relative positions of the atoms in …

CHARMM (Chemistry at HARvard Molecular Mechanics) is a highly versatile and widely
used molecular simulation program. It has been developed over the last three decades with a …

A combined quantum mechanical (QM) and molecular mechanical (MM) potential has been
developed for the study of reactions in condensed phases. For the quantum mechanical …

THE number of all possible conformations of a polypeptide chain is too large to be sampled
exhaustively. Nevertheless, protein sequences do fold into unique native states in seconds (…

(1) Most of the calculations reported in this paper were made on ILLIAC at the University of
Illinois during the year 1959-1960 and reported at the American Chemical Society …

The valence‐bond theory for the contact electron‐spin coupling of nuclear magnetic moments
is used to calculate the proton‐proton, proton‐fluorine, and fluorine‐fluorine coupling …