Bruce Tidor

TL;DR: An overview of the CHARMM program as it exists today is provided with an emphasis on developments since the publication of the original CHARMM article in 1983.

TL;DR: Model building suggests that the arginine eta nitrogens and the epsilon nitrogen can form specific networks of hydrogen bonds with adjacent pairs of phosphates and that these arrangements are likely to occur near RNA loops and bulges and not within double-stranded A-form RNA.

TL;DR: The electrostatic contribution to the free energy of folding was calculated fo 21 salt bridges in 9 r X‐ray crystal structures using a continuum electrostatic approach with the DELPHI computer‐program package, which found the majority were found to be electrostatically destabilizing.

TL;DR: The de novo design of a family of alpha-helical bundle proteins with a right-handed superhelical twist is described, where the overall protein fold was specified by hydrophobic-polar residue patterning, whereas the bundle oligomerization state, detailed main-chain conformation, and interior side-chain rotamers were engineered by computational enumerations of packing in alternate backbone structures.

TL;DR: An iterative computational design procedure that focuses on electrostatic binding contributions and single mutants for enhancing and accelerating the development of protein reagents and therapeutics is presented.