The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State
Author:
Funder
National Science Foundation
Publisher
Elsevier BV
Subject
Biophysics
Reference50 articles.
1. Crystal structure of prokaryotic ribosomal protein L9: a bi-lobed RNA-binding protein;Hoffman;EMBO J.,1994
2. Global analysis of the effects of temperature and denaturant on the folding and unfolding kinetics of the N-terminal domain of the protein L9;Kuhlman;J. Mol. Biol.,1998
3. Surface salt bridges, double-mutant cycles, and protein stability: an experimental and computational analysis of the interaction of the Asp 23 side chain with the N-terminus of the N-terminal domain of the ribosomal protein L9;Luisi;Biochemistry,2003
4. 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 folding;Luisi;J. Mol. Biol.,2000
5. Kinetic isotope effects reveal the presence of significant secondary structure in the transition state for the folding of the N-terminal domain of L9;Sato;J. Mol. Biol.,2007
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