B
Bruce Tidor
Researcher at Massachusetts Institute of Technology
Publications - 180
Citations - 19350
Bruce Tidor is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Protease & Binding site. The author has an hindex of 60, co-authored 179 publications receiving 17680 citations. Previous affiliations of Bruce Tidor include National University of Singapore & Harvard University.
Papers
More filters
Proceedings Article
An Analysis of Selection Procedures with Particular Attention Paid to Proportional and Boltzmann Selection
Michael de la Maza,Bruce Tidor +1 more
Journal ArticleDOI
Side-chain repacking calculations for predicting structures and stabilities of heterodimeric coiled coils.
TL;DR: The results show that computational methods can predict interaction specificities that are in good agreement with experimental data.
Journal ArticleDOI
Optimizing electrostatic affinity in ligand-receptor binding: Theory, computation, and ligand properties
Erik Kangas,Bruce Tidor +1 more
TL;DR: Lee et al. as discussed by the authors developed a theoretical framework for analyzing the tradeoff between an unfavorable electrostatic desolvation penalty incurred when the ligand binds a receptor in aqueous solution and the generally favorable intermolecular interactions made in the bound state.
Journal ArticleDOI
Probing the roles of residues at the e and g positions of the GCN4 leucine zipper by combinatorial mutagenesis.
TL;DR: These studies suggest that the identities of surface side chains at the e and g positions of coiled coils contribute modestly to stability; by comparison with previous work, however, the eand g positions are far less critical than residues at the a and d positions, which form the hydrophobic core of the dimer interface.
Journal ArticleDOI
Effects of salt bridges on protein structure and design
TL;DR: An energy function for simple cubic lattice polymers based on continuum electrostatic calculations of a representative selection of salt bridges found in known protein crystal structures demonstrates that, while the more highly charged sequences are less stable, the loss of stability is accompanied by a substantial reduction in the degeneracy of the lowest‐energy state.