pH-dependent Stability and Folding Kinetics of a Protein with an Unusual α–β Topology: The C-terminal Domain of the Ribosomal Protein L9
- 26 April 2002
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 318 (2), 571-582
- https://doi.org/10.1016/s0022-2836(02)00015-3
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- The pK a of His-24 in the folding transition state of apomyoglobinProceedings of the National Academy of Sciences, 2001
- Ph-dependent interactions and the stability and folding kinetics of the N-terminal domain of L9. electrostatic interactions are only weakly formed in the transition state for foldingJournal of Molecular Biology, 2000
- Finding the right fold.Nature Structural & Molecular Biology, 1999
- Ribosomal Protein L9: A Structure Determination by the Combined Use of X-ray Crystallography and NMR SpectroscopyJournal of Molecular Biology, 1996
- Titration Properties and Thermodynamics of the Transition State for Folding: Comparison of Two-state and Multi-state Folding PathwaysJournal of Molecular Biology, 1996
- Formation of Electrostatic Interactions on the Protein-Folding PathwayBiochemistry, 1996
- Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding.Proceedings of the National Academy of Sciences, 1994
- The folding of an enzymeJournal of Molecular Biology, 1992
- Mapping the transition state and pathway of protein folding by protein engineeringNature, 1989
- Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigationsBiochemistry, 1989