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Comment
. 2008 Nov 4;105(44):16825-6.
doi: 10.1073/pnas.0809224105. Epub 2008 Oct 30.

Protein denaturation by urea: slash and bond

Affiliations
Comment

Protein denaturation by urea: slash and bond

Peter J Rossky. Proc Natl Acad Sci U S A. .
No abstract available

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Conflict of interest statement

The author declares no conflict of interest.

Figures

Fig. 1.
Fig. 1.
Electrostatic potentials mapped onto the surface of a simplified secondary structure cylinder representation (Left) and onto the solvent-accessible surface area of each helix (Right; cylindrical helices yellow) in the core formed by the A, G, and H helices in apomyoglobin (17). Electrostatic potentials from red to blue correspond to the range −5 kT/e to +5 kT/e, where k is Boltzmann's constant, e is the magnitude of the electron charge, and T is taken as 298 K. (Figure courtesy of Dr. Carlos F. Lopez, Department of Systems Biology, Harvard Medical School, Boston.)

Comment on

References

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