Prediction of Catalytic Residues in Enzymes Based on Known Tertiary Structure, Stability Profile, and Sequence Conservation
- 1 April 2003
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 327 (5) , 1053-1064
- https://doi.org/10.1016/s0022-2836(03)00207-9
Abstract
No abstract availableKeywords
Funding Information
- Ministry of Education, Culture, Sports, Science and Technology
This publication has 51 references indexed in Scilit:
- Prediction of functionally important residues based solely on the computed energetics of protein structure 1 1Edited by B. HonigJournal of Molecular Biology, 2001
- ConSurf: an algorithmic tool for the identification of functional regions in proteins by surface mapping of phylogenetic informationJournal of Molecular Biology, 2001
- The Protein Data BankNucleic Acids Research, 2000
- Gapped BLAST and PSI-BLAST: a new generation of protein database search programsNucleic Acids Research, 1997
- Predicting protein stability changes upon mutation using database-derived potentials: solvent accessibility determines the importance of local versus non-local interactions along the sequenceJournal of Molecular Biology, 1997
- An Evolutionary Trace Method Defines Binding Surfaces Common to Protein FamiliesJournal of Molecular Biology, 1996
- Prediction of Protein Secondary Structure by Combining Nearest-neighbor Algorithms and Multiple Sequence AlignmentsJournal of Molecular Biology, 1995
- CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choiceNucleic Acids Research, 1994
- Protein Secondary Structure Prediction Using Nearest-neighbor MethodsJournal of Molecular Biology, 1993
- Effect of active site residues in barnase on activity and stabilityJournal of Molecular Biology, 1992