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Comment
. 2010 Oct 12;107(41):17457-8.
doi: 10.1073/pnas.1013095107. Epub 2010 Oct 6.

Crowding and function reunite

Gary J Pielak  1 , Andrew C Miklos
Affiliations
Comment

Crowding and function reunite

Gary J Pielak et al. Proc Natl Acad Sci U S A. .
No abstract available

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Fig. 1.
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).
See this image and copyright information in PMC

Comment on

References

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    1. Dhar A, et al. Structure, function, and folding of phosphoglycerate kinase are strongly perturbed by macromolecular crowding. Proc Natl Acad Sci USA. 2010;107:17586–17591. - PMC - PubMed
    1. Ogston AG. The spaces in a uniform random suspension of fibres. Trans Faraday Soc. 1958;54:1754–1757.
    1. Ogston AG, Phelps CF. The partition of solutes between buffer solutions and solutions containing hyaluronic acid. Biochem J. 1961;78:827–833. - PMC - PubMed
    1. 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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