Prediction of the disulfide-bonding state of cysteines in proteins based on dipeptide composition
- 1 May 2004
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 318 (1) , 142-147
- https://doi.org/10.1016/j.bbrc.2004.03.189
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- A Novel Database of Disulfide Patterns and its Application to the Discovery of Distantly Related HomologsJournal of Molecular Biology, 2004
- What can Disulfide Bonds Tell Us about Protein Energetics, Function and Folding: Simulations and Bioninformatics AnalysisJournal of Molecular Biology, 2000
- The Protein Data BankNucleic Acids Research, 2000
- Ab Initio fold prediction of small helical proteins using distance geometry and knowledge-based scoring functionsJournal of Molecular Biology, 1999
- MONSSTER: a method for folding globular proteins with a small number of distance restraintsJournal of Molecular Biology, 1997
- Analysis and Classification of Disulphide Connectivity in ProteinsJournal of Molecular Biology, 1994
- Determination of the disulfide bridges in factor Va heavy chainBiochemistry, 1994
- Different sequence environments of cysteines and half cystines in proteins Application to predict disulfide forming residuesFEBS Letters, 1992
- Protein engineering of a disulfide bond in a .beta./.alpha.-barrel proteinBiochemistry, 1992
- A new method for rapid assignment of S-S bridges in proteinsBiochemical and Biophysical Research Communications, 1985