Crowding and function reunite - PubMed (original) (raw)
Comment
Crowding and function reunite
Gary J Pielak et al. Proc Natl Acad Sci U S A. 2010.
No abstract available
Conflict of interest statement
The authors declare no conflict of interest.
Figures
Fig. 1.
(A) The Escherichia coli cytoplasm, as modeled by McGuffee and Elcock (1). (B) Open form of phosphoglycerate kinase (PDB ID code 1QPG), visualized with visual molecular dynamics (20).
Comment on
- Structure, function, and folding of phosphoglycerate kinase are strongly perturbed by macromolecular crowding.
Dhar A, Samiotakis A, Ebbinghaus S, Nienhaus L, Homouz D, Gruebele M, Cheung MS. Dhar A, et al. Proc Natl Acad Sci U S A. 2010 Oct 12;107(41):17586-91. doi: 10.1073/pnas.1006760107. Epub 2010 Oct 4. Proc Natl Acad Sci U S A. 2010. PMID: 20921368 Free PMC article.
References
- Ogston AG. The spaces in a uniform random suspension of fibres. Trans Faraday Soc. 1958;54:1754–1757.
- Minton AP, Wilf J. Effect of macromolecular crowding upon the structure and function of an enzyme: Glyceraldehyde-3-phosphate dehydrogenase. Biochemistry. 1981;20:4821–4826. - PubMed
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