Characterisation of the Conformational Properties of Urea-unfolded Im7: Implications for the Early Stages of Protein Folding
- 8 December 2006
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 364 (4) , 824-835
- https://doi.org/10.1016/j.jmb.2006.09.037
Abstract
No abstract availableKeywords
This publication has 63 references indexed in Scilit:
- Unfolded Proteins and Protein Folding Studied by NMRChemical Reviews, 2004
- Coupling of folding and binding for unstructured proteinsCurrent Opinion in Structural Biology, 2002
- Persistence of Native-Like Topology in a Denatured Protein in 8 M UreaScience, 2001
- Intrinsically unstructured proteins: re-assessing the protein structure-function paradigmJournal of Molecular Biology, 1999
- Structural mobility of the human prion protein probed by backbone hydrogen exchange.Nature Structural & Molecular Biology, 1999
- Structural and Dynamical Properties of a Denatured Protein. Heteronuclear 3D NMR Experiments and Theoretical Simulations of Lysozyme in 8 M UreaBiochemistry, 1997
- The denatured state (the other half of the folding equation) and its role in protein stabilityThe FASEB Journal, 1996
- A Comparison of the pH, Urea, and Temperature-denatured States of Barnase by Heteronuclear NMR: Implications for the Initiation of Protein FoldingJournal of Molecular Biology, 1995
- Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications.Proceedings of the National Academy of Sciences, 1995
- Structural Characterization of the FK506 Binding Protein Unfolded in Urea and Guanidine HydrochlorideJournal of Molecular Biology, 1994