Computer simulation of protein folding
- 1 February 1975
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 253 (5494) , 694-698
- https://doi.org/10.1038/253694a0
Abstract
A new and very simple representation of protein conformations has been used together with energy minimisation and thermalisation to simulate protein folding. Under certain conditions, the method succeeds in ‘renaturing’ bovine pancreatic trypsin inhibitor from an open-chain conformation into a folded conformation close to that of the native molecule.Keywords
This publication has 8 references indexed in Scilit:
- The single-disulphide intermediates in the refolding of reduced pancreatic trypsin inhibitorJournal of Molecular Biology, 1974
- Comparison of predicted and experimentally determined secondary structure of adenyl kinaseNature, 1974
- Refinement of the x-ray structure of lysozyme by complete energy minimizationBiochemistry, 1974
- Principles that Govern the Folding of Protein ChainsScience, 1973
- Pancreatic Trypsin Inhibitor (Kunitz): Part I: Structure and functionCold Spring Harbor Symposia on Quantitative Biology, 1972
- Microscopic model for the study of fluctuations and the kinetics of conformational changes of polypeptides. I. DiglycineBiopolymers, 1971
- Refinement of protein conformations using a macromolecular energy minimization procedureJournal of Molecular Biology, 1969