Watching protein folding unfold
- 1 October 1995
- journal article
- research article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 2 (10) , 817-820
- https://doi.org/10.1038/nsb1095-817
Abstract
Direct NMR observation of a transient folding intermediate provides new evidence for the importance of molten globules as general intermediates in protein folding.Keywords
This publication has 60 references indexed in Scilit:
- Following protein folding in real time using NMR spectroscopyNature Structural & Molecular Biology, 1995
- Probing the structure of folding intermediatesCurrent Opinion in Structural Biology, 1994
- Protein folding and stability: the pathway of folding of barnaseFEBS Letters, 1993
- PATHWAYS OF PROTEIN FOLDINGAnnual Review of Biochemistry, 1993
- Transient folding intermediates characterized by protein engineeringNature, 1990
- INTERMEDIATES IN THE FOLDING REACTIONS OF SMALL PROTEINSAnnual Review of Biochemistry, 1990
- 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
- [22] Structural characterization of protein folding intermediates by proton magnetic resonance and hydrogen exchangePublished by Elsevier ,1989
- [26] Effect of point mutations of the folding of globular proteinsPublished by Elsevier ,1987