Catalytic Versatility, Stability, and Evolution of the (βα)8-Barrel Enzyme Fold
- 1 November 2005
- journal article
- review article
- Published by American Chemical Society (ACS) in Chemical Reviews
- Vol. 105 (11) , 4038-4055
- https://doi.org/10.1021/cr030191z
Abstract
No abstract availableThis publication has 156 references indexed in Scilit:
- An Obligatory Intermediate Controls the Folding of the α-Subunit of Tryptophan Synthase, a TIM Barrel ProteinJournal of Molecular Biology, 2005
- Protein Sequence Randomization: Efficient Estimation of Protein Stability Using Knowledge-based PotentialsJournal of Molecular Biology, 2005
- Directed evolution of enzymes for biocatalysis and the life sciencesCellular and Molecular Life Sciences, 2004
- Mapping of Unit Boundaries of a Protein: Exhaustive Search for Permissive Sites for Duplication by Complementation Analysis of Random Fragment Libraries of Tryptophan Synthase α SubunitJournal of Molecular Biology, 2004
- The equilibrium unfolding pathway of a (β/α)8 barrelJournal of Molecular Biology, 2002
- Crystal Structure of Human Renal Dipeptidase Involved in β-Lactam HydrolysisJournal of Molecular Biology, 2002
- Crystal structure of activated ribulose-1,5-bisphosphate carboxylase/oxygenase from green alga Chlamydomonas reinhardtii complexed with 2-carboxyarabinitol-1,5-bisphosphateJournal of Molecular Biology, 2002
- The structure of Escherichia coli cytosine deaminase 1 1Edited by I. A. WilsonJournal of Molecular Biology, 2002
- The transition between the open and closed states of rubisco is triggered by the inter-phosphate distance of the bound bisphosphateJournal of Molecular Biology, 2000
- De Novo protein design: towards fully automated sequence selection 1 1Edited by P. E. WrightJournal of Molecular Biology, 1997