Effect of Multiple Prolyl Isomerization Reactions on the Stability and Folding Kinetics of the Notch Ankyrin Domain: Experiment and Theory
- 16 September 2005
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 352 (2) , 253-265
- https://doi.org/10.1016/j.jmb.2005.06.041
Abstract
No abstract availableKeywords
Funding Information
- National Institutes of Health
This publication has 42 references indexed in Scilit:
- Experimental Characterization of the Folding Kinetics of the Notch Ankyrin DomainJournal of Molecular Biology, 2005
- Structure and stability of the ankyrin domain of the Drosophila Notch receptorProtein Science, 2003
- Stability and folding of the tumour suppressor protein p16 1 1Edited by J. KarnJournal of Molecular Biology, 1999
- Contact order, transition state placement and the refolding rates of single domain proteins 1 1Edited by P. E. WrightJournal of Molecular Biology, 1998
- Structure of the p53 Tumor Suppressor Bound to the Ankyrin and SH3 Domains of 53BP2Science, 1996
- HEAT repeats in the Huntington's disease proteinNature Genetics, 1995
- Kinetic coupling between protein folding and prolyl isomerizationJournal of Molecular Biology, 1992
- Kinetic coupling between protein folding and prolyl isomerizationJournal of Molecular Biology, 1992
- Proline isomerization during refolding of ribonuclease A is accelerated by the presence of folding intermediatesFEBS Letters, 1986
- The rate of interconversion between the two unfolded forms of ribonuclease A does not depend on guanidinium chloride concentrationJournal of Molecular Biology, 1979