Sequence conservation provides the best prediction of the role of proline residues in p13suc1
- 4 August 2000
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 301 (1) , 199-204
- https://doi.org/10.1006/jmbi.2000.3958
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- Helix geometry in proteinsPublished by Elsevier ,2004
- Decreasing the stability and changing the substrate specificity of the Bacillus stearothermophilus alcohol dehydrogenase by single amino acid replacementsProtein Engineering, Design and Selection, 1998
- Structural and functional roles of a conserved proline residue in the alpha2 helix of Escherichia coli thioredoxinProtein Engineering, Design and Selection, 1997
- Crystal Structure and Mutational Analysis of the Human CDK2 Kinase Complex with Cell Cycle–Regulatory Protein CksHs1Cell, 1996
- Crystal structure of the cell cycle-regulatory protein suc1 reveals a beta-hinge conformational switch.Proceedings of the National Academy of Sciences, 1995
- Stabilization of Bacillus stearothermophilus neutral protease by introduction of prolinesFEBS Letters, 1993
- Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with x-ray structure analysis of proline mutantsBiochemistry, 1992
- Non-additivity in protein-protein interactionsJournal of Molecular Biology, 1987
- Sucl+ encodes a predicted 13-kilodalton protein that is essential for cell viability and is directly involved in the division cycle of Schizosaccharomyces pombe.Molecular and Cellular Biology, 1987
- The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus)Cell, 1984