Molecular dynamics simulations of apocytochrome b562– the highly ordered limit of molten globules
- 1 October 1996
- journal article
- Published by Elsevier in Folding and Design
- Vol. 1 (5), 335-346
- https://doi.org/10.1016/s1359-0278(96)00049-1
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Nuclear magnetic resonance chemical shift: comparison of estimated secondary structures in peptides by nuclear magnetic resonance and circular dichroismProtein Engineering, Design and Selection, 1996
- Potential energy function and parameters for simulations of the molecular dynamics of proteins and nucleic acids in solutionComputer Physics Communications, 1995
- Molecular Dynamics Simulations of Protein Unfolding and Limited Refolding: Characterization of Partially Unfolded States of Ubiquitin in 60% Methanol and in WaterJournal of Molecular Biology, 1995
- Protein Unfolding Pathways Explored Through Molecular Dynamics SimulationsJournal of Molecular Biology, 1993
- Characterization of “native” apomyoglobin by molecular dynamics simulationJournal of Molecular Biology, 1992
- Molecular dynamics simulations of helix denaturationJournal of Molecular Biology, 1992
- A molecular dynamics simulation of polyalanine: An analysis of equilibrium motions and helix–coil transitionsBiopolymers, 1991
- The MIDAS display systemJournal of Molecular Graphics, 1988
- Improvement of the 2.5 Å resolution model of cytochrome b562 by redetermining the primary structure and using molecular graphicsJournal of Molecular Biology, 1981
- The interpretation of protein structures: Estimation of static accessibilityJournal of Molecular Biology, 1971