Testing the role of chain connectivity on the stability and structure of dihydrofolate reductase fromE. coli: Fragment complementation and circular permutation reveal stable, alternatively folded forms
Open Access
- 1 January 2001
- journal article
- Published by Wiley in Protein Science
- Vol. 10 (1) , 116-128
- https://doi.org/10.1110/ps.26601
Abstract
Protein Science, the flagship journal of The Protein Society, serves an international forum for publishing original reports on all scientific aspects of protein molecules. The Journal publishes papers by leading scientists from all over the world that report on advances in the understanding of proteins in the broadest sense. Protein Science aims to unify this field by cutting across established disciplinary lines and focusing on “protein-centered” science.Keywords
This publication has 63 references indexed in Scilit:
- Circular permutation within the coenzyme binding domain of the tetrameric glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilusProtein Science, 2008
- Eye lens βB2-crystallin: circular permutation does not influence the oligomerization state but enhances the conformational stabilityJournal of Molecular Biology, 1998
- Folding of Circular and Permuted Chymotrypsin Inhibitor 2: Retention of the Folding NucleusBiochemistry, 1998
- Probing minimal independent folding units in dihydrofolate reductase by molecular dissectionProtein Science, 1997
- Detection of a Stable Intermediate in the Thermal Unfolding of a Cysteine-Free Form of Dihydrofolate Reductase from Escherichia ColiBiochemistry, 1995
- Analysis of the mechanism of assembly of cleaved barnase from two peptide fragments and its relevance to the folding pathway of uncleaved barnaseBiochemistry, 1995
- Folding of Barnase in PartsBiochemistry, 1994
- A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: Verification and refinement of a four-channel modelBiochemistry, 1993
- Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopyBiochemistry, 1991
- Mitochondrial protein import: Nucleoside triphosphates are involved in conferring import-competence to precursorsCell, 1987