Conformational specificity of trigger factor for the folding intermediates of α-lactalbumin
- 12 July 2000
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1480 (1-2) , 77-82
- https://doi.org/10.1016/s0167-4838(00)00094-7
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- Recognition of protein substrates by the prolyl isomerase trigger factor is independent of proline residuesJournal of Molecular Biology, 1998
- Assisted Protein FoldingJournal of Biological Chemistry, 1997
- Structures of folding intermediatesCurrent Opinion in Structural Biology, 1995
- Pathway of disulfide-coupled unfolding and refolding of bovine .alpha.-lactalbuminBiochemistry, 1993
- Protein folding in the cellNature, 1992
- Study of the “molten globule” intermediate state in protein folding by a hydrophobic fluorescent probeBiopolymers, 1991
- Dissociation and aggregation of d-glyceraldehyde-3-phosphate dehydrogenase during denaturation by guanidine hydrochlorideBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990
- Evidence for a molten globule state as a general intermediate in protein foldingFEBS Letters, 1990
- ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particleCell, 1988
- Kinetic aspects of conformational changes in proteins. I. Rate of regain of enzyme activity from denatured proteinsBiochemistry, 1971