AFM structural study of the molecular chaperone GroEL and its two-dimensional crystals: an ideal “living” calibration sample
- 31 October 2002
- journal article
- Published by Elsevier in Ultramicroscopy
- Vol. 93 (1) , 83-89
- https://doi.org/10.1016/s0304-3991(02)00149-3
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- Structural Changes of theEscherichia coliGroEL–GroES Chaperonins upon Complex Formation in Solution: A Neutron Small Angle Scattering StudyJournal of Structural Biology, 1998
- Atomic Force Microscopy Detects Changes in the Interaction Forces between GroEL and Substrate ProteinsBiophysical Journal, 1998
- Visualization of supercoiled DNA with atomic force microscopy in situProceedings of the National Academy of Sciences, 1997
- The Chaperonin ATPase Cycle: Mechanism of Allosteric Switching and Movements of Substrate-Binding Domains in GroELCell, 1996
- Molecular chaperones in cellular protein foldingNature, 1996
- High resolution surface structure of E. coli GroES oligomer by atomic force microscopyFEBS Letters, 1996
- Asymmetrical Interaction of GroEL and GroES in the ATPase Cycle of Assisted Protein FoldingScience, 1995
- Force-induced conformational change of bacteriorhodopsinJournal of Molecular Biology, 1995
- Direct Observation of Enzyme Activity with the Atomic Force MicroscopeScience, 1994
- Atomic Force MicroscopePhysical Review Letters, 1986