The Low-pH Unfolded State of the C-Terminal Domain of the Ribosomal Protein L9 Contains Significant Secondary Structure in the Absence of Denaturant but Is No More Compact Than the Low-pH Urea Unfolded State
- 16 August 2008
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 47 (36) , 9565-9573
- https://doi.org/10.1021/bi8006862
Abstract
No abstract availableKeywords
This publication has 40 references indexed in Scilit:
- Sensitivity of secondary structure propensities to sequence differences between α‐ and γ‐synuclein: Implications for fibrillationProtein Science, 2006
- Solution structure of a protein denatured state and folding intermediateNature, 2005
- Mutational Analysis Demonstrates that Specific Electrostatic Interactions can Play a Key Role in the Denatured State Ensemble of ProteinsJournal of Molecular Biology, 2005
- Direct Characterization of the Folded, Unfolded and Urea-denatured States of the C-terminal Domain of the Ribosomal Protein L9Journal of Molecular Biology, 2005
- Intrinsically unstructured proteins and their functionsNature Reviews Molecular Cell Biology, 2005
- Dynamics in the Unfolded State of β2-microglobulin Studied by NMRJournal of Molecular Biology, 2005
- Thermodynamics and Kinetics of Non-native Interactions in Protein Folding: A Single Point Mutant Significantly Stabilizes the N-terminal Domain of L9 by Modulating Non-native Interactions in the Denatured StateJournal of Molecular Biology, 2004
- Calculation of ensembles of structures representing the unfolded state of an SH3 domainJournal of Molecular Biology, 2001
- NMR Studies of Unfolded States of an SH3 Domain in Aqueous Solution and Denaturing ConditionsBiochemistry, 1997
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995