Characterization of “native” apomyoglobin by molecular dynamics simulation
- 20 September 1992
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 227 (2) , 375-380
- https://doi.org/10.1016/0022-2836(92)90893-o
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- Vector and parallel algorithms for the molecular dynamics simulation of macromolecules on shared‐memory computersJournal of Computational Chemistry, 1991
- Probing the stability of a partly folded apomyoglobin intermediate by site-directed mutagenesisBiochemistry, 1991
- Molecular dynamics simulations of the unfolding of an .alpha.-helical analog of ribonuclease A S-peptide in waterBiochemistry, 1991
- Use of site-directed mutagenesis to destabilize native apomyoglobin relative to folding intermediatesBiochemistry, 1989
- Thermodynamic study of the apomyoglobin structureJournal of Molecular Biology, 1988
- Comparison of simple potential functions for simulating liquid waterThe Journal of Chemical Physics, 1983
- CHARMM: A program for macromolecular energy, minimization, and dynamics calculationsJournal of Computational Chemistry, 1983
- Structure and refinement of oxymyoglobin at 1·6 Å resolutionJournal of Molecular Biology, 1980
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977
- Principles that Govern the Folding of Protein ChainsScience, 1973