Cooperative folding of the isolated α-helical domain of hen egg-white lysozyme
- 23 November 2001
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 314 (2) , 321-329
- https://doi.org/10.1006/jmbi.2001.5122
Abstract
No abstract availableKeywords
This publication has 48 references indexed in Scilit:
- Intermediates can accelerate protein foldingProceedings of the National Academy of Sciences, 1999
- Characterization of transient intermediates in lysozyme folding with time-resolved small-angle X-ray scatteringJournal of Molecular Biology, 1999
- The folding process of hen lysozyme: a perspective from the ‘new view’Cellular and Molecular Life Sciences, 1998
- Kinetics of lysozyme refolding: structural characterization of a non-specifically collapsed state using time-resolved X-ray scatteringJournal of Molecular Biology, 1998
- Nucleation mechanisms in protein foldingCurrent Opinion in Structural Biology, 1997
- Kinetic role of early intermediates in protein foldingCurrent Opinion in Structural Biology, 1997
- On-pathway versus off-pathway folding intermediatesFolding and Design, 1996
- The molten globule state of α‐lactalbuminThe FASEB Journal, 1996
- Crystal structure of human α-lactalbumin at 1·7 Å resolutionJournal of Molecular Biology, 1991
- Refined structure of baboon α-lactalbumin at 1.7 Å resolutionJournal of Molecular Biology, 1989