Congo red-stabilized intermediates in the λ light chain transition from native to molten state
- 1 January 1996
- Vol. 78 (3) , 183-189
- https://doi.org/10.1016/0300-9084(96)89503-4
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Does the molten globule have a native-like tertiary fold?Philosophical Transactions Of The Royal Society B-Biological Sciences, 1995
- Residual Structure in a Staphylococcal Nuclease FragmentJournal of Molecular Biology, 1994
- Thermodynamic Puzzle of Apomyoglobin UnfoldingJournal of Molecular Biology, 1994
- Further Examination of the Intermediate State in the Denaturation of the Tryptophan Synthase α SubunitJournal of Molecular Biology, 1993
- Are the Molten Globule and the Unfolded States of Apo-α-Lactalbumin Enthalpically Equivalent?Journal of Molecular Biology, 1993
- PATHWAYS OF PROTEIN FOLDINGAnnual Review of Biochemistry, 1993
- Structural energetics of the molten globule stateProteins-Structure Function and Bioinformatics, 1993
- Heat and cold denaturation of β‐lactoglobulin BFEBS Letters, 1992
- Evidence for a molten globule state as a general intermediate in protein foldingFEBS Letters, 1990
- The molten globule state as a clue for understanding the folding and cooperativity of globular‐protein structureProteins-Structure Function and Bioinformatics, 1989