The High-Resolution NMR Structure of the Early Folding Intermediate of the Thermus thermophilus Ribonuclease H
- 26 September 2008
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 384 (2) , 531-539
- https://doi.org/10.1016/j.jmb.2008.09.044
Abstract
No abstract availableKeywords
This publication has 55 references indexed in Scilit:
- Predicting protein folding rates from geometric contact and amino acid sequenceProtein Science, 2008
- Protein folding and misfolding: mechanism and principlesQuarterly Reviews of Biophysics, 2007
- The Folding Pathway of T4 Lysozyme: The High-resolution Structure and Folding of a Hidden IntermediateJournal of Molecular Biology, 2007
- Intermediates: ubiquitous species on folding energy landscapes?Current Opinion in Structural Biology, 2007
- Fast and Slow Intermediate Accumulation and the Initial Barrier Mechanism in Protein FoldingJournal of Molecular Biology, 2002
- Topological and energetic factors: what determines the structural details of the transition state ensemble and “en-route” intermediates for protein folding? an investigation for small globular proteinsJournal of Molecular Biology, 2000
- Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation ModelingBiophysical Journal, 2000
- Contact order, transition state placement and the refolding rates of single domain proteins 1 1Edited by P. E. WrightJournal of Molecular Biology, 1998
- AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMRJournal of Biomolecular NMR, 1996
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995