Mixed Macromolecular Crowding Accelerates the Oxidative Refolding of Reduced, Denatured Lysozyme
Open Access
- 1 December 2004
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 279 (53) , 55109-55116
- https://doi.org/10.1074/jbc.m409086200
Abstract
No abstract availableKeywords
This publication has 48 references indexed in Scilit:
- Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coliPublished by Elsevier ,2005
- Protein folding and misfoldingNature, 2003
- The Place of Inactivated Actin and Its Kinetic Predecessor in Actin Folding−UnfoldingBiochemistry, 2002
- Effects of Macromolecular Crowding on the Refolding of Glucose- 6-phosphate Dehydrogenase and Protein Disulfide IsomeraseJournal of Biological Chemistry, 2001
- Excluded Volume Effects on the Refolding and Assembly of an Oligomeric ProteinJournal of Biological Chemistry, 2001
- Characterisation of the dominant oxidative folding intermediate of hen lysozyme 1 1Edited by P. E. WrightJournal of Molecular Biology, 1999
- Three-state model for lysozyme folding: triangular folding mechanism with an energetically trapped intermediateJournal of Molecular Biology, 1997
- Fast and slow tracks in lysozyme folding: insight into the role of domains in the folding processJournal of Molecular Biology, 1997
- Kinetic resolution of peptide bond and side chain far-UV circular dichroism during the folding of hen egg white lysozymeBiochemistry, 1992
- Principles that Govern the Folding of Protein ChainsScience, 1973