Journal article
Atomic-level observation of macromolecular crowding effects: escape of a protein from the GroEL cage
Proceedings of the National Academy of Sciences - PNAS, Vol.100(5), pp.2340-2344
03/04/2003
DOI: 10.1073/pnas.0535055100
PMCID: PMC151342
PMID: 12601146
Abstract
Experimental work has demonstrated that the efficient operation of the GroEL-GroES chaperonin machinery is sensitive to the presence of macromolecular crowding agents. Here, I describe atomically detailed computer simulations that provide a microscopic view of how crowding effects are exerted. Simulations were performed to compute the free energy required to extract the protein rhodanese from the central cavity of GroEL into solutions containing a range of crowder concentrations. The computed energetics allow the total yield of folded protein to be predicted; the calculated yields show a nonlinear dependence on the concentration of crowding agent identical to that observed experimentally. The close correspondence between simulation and experiment prompts the use of the former in a truly predictive setting: simulations are used to suggest that more effective crowding agents might be designed by exploiting an "agoraphobic effect."
Details
- Title: Subtitle
- Atomic-level observation of macromolecular crowding effects: escape of a protein from the GroEL cage
- Creators
- Adrian H Elcock - Department of Biochemistry, University of Iowa, Iowa City, IA 52242, USA. adrian-elcock@uiowa.edu
- Resource Type
- Journal article
- Publication Details
- Proceedings of the National Academy of Sciences - PNAS, Vol.100(5), pp.2340-2344
- DOI
- 10.1073/pnas.0535055100
- PMID
- 12601146
- PMCID
- PMC151342
- NLM abbreviation
- Proc Natl Acad Sci U S A
- ISSN
- 0027-8424
- eISSN
- 1091-6490
- Publisher
- National Academy of Sciences; United States
- Language
- English
- Date published
- 03/04/2003
- Academic Unit
- Physics and Astronomy; Biochemistry and Molecular Biology
- Record Identifier
- 9984024562402771
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