Protein Compactness Measured by Fluorescence Resonance Energy Transfer
Open Access
- 1 June 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (24) , 21765-21775
- https://doi.org/10.1074/jbc.m010858200
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complexNature, 1997
- Refolding and Reassociation of Glycerol Dehydrogenase from Bacillus Stearothermophilus in the Absence and Presence of GroelEuropean Journal of Biochemistry, 1996
- Dynamics of the GroEL – Protein Complex: Effects of Nucleotides and Folding MutantsJournal of Molecular Biology, 1996
- GroEL/ES-mediated refolding of human carbonic anhydrase II: role of N-terminal helices as recognition motifs for GroELBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1995
- Roles of molecular chaperones in protein foldingCurrent Opinion in Structural Biology, 1994
- The crystal structure of the bacterial chaperonln GroEL at 2.8 ÅNature, 1994
- Heat‐shock proteins as molecular chaperonesEuropean Journal of Biochemistry, 1994
- Refolding of Barnase in the Presence of GroEJournal of Molecular Biology, 1993
- Protein folding in the cellNature, 1992
- Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNANature, 1978