An optimized strategy to measure protein stability highlights differences between cold and hot unfolded states-Reference-Cited by-同舟云学术

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An optimized strategy to measure protein stability highlights differences between cold and hot unfolded states

Published:2017-05-18 Issue:1 Volume:8 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

Author:

Alfano Caterina,Sanfelice Domenico,Martin Stephen R.,Pastore Annalisa,Temussi Piero Andrea

Publisher

Springer Science and Business Media LLC

Subject

General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry

Link

http://www.nature.com/articles/ncomms15428.pdf

Reference46 articles.

1. Zimmerman, S. B. & Trach, S. O. Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli. J. Mol. Biol. 222, 599–620 (1991).

2. Politou, A. & Temussi, P. A. Revisiting a dogma: the effect of volume exclusion in molecular crowding. Curr. Opin. Struct. Biol. 30, 1–6 (2015).

3. Hong, J. & Gierasch, L. M. Macromolecular crowding remodels the energy landscape of a protein by favoring a more compact unfolded state. J. Am. Chem. Soc. 132, 10445–10452 (2010).

4. Smith, A. E., Zhang, Z., Pielak, G. J. & Li, C. NMR studies of protein folding and binding in cells and cell-like environments. Curr. Opin. Struct. Biol. 30, 7–16 (2015).

5. Oshima, H. & Kinoshita, M. Effects of sugars on the thermal stability of a protein. J. Chem. Phys. 138, 245101 (2013).

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