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Cold unfolding of β-hairpins: a molecular-level rationalization.
Riccio A, Graziano G. Riccio A, et al. Among authors: graziano g. Proteins. 2011 Jun;79(6):1739-46. doi: 10.1002/prot.22997. Epub 2011 Apr 4. Proteins. 2011. PMID: 21465553
It is shown that a molecular-level rationalization of this cold unfolding can be provided extending the approach devised for globular proteins (Graziano G. Phys Chem Chem Phys 2010; 12:14245-14252). The decrease in the solvent-excluded volume upon folding, measured …
It is shown that a molecular-level rationalization of this cold unfolding can be provided extending the approach devised for globular protei …
Contrasting the denaturing effect of guanidinium chloride with the stabilizing effect of guanidinium sulfate.
Graziano G. Graziano G. Phys Chem Chem Phys. 2011 Jul 7;13(25):12008-14. doi: 10.1039/c1cp20843h. Epub 2011 May 27. Phys Chem Chem Phys. 2011. PMID: 21617819
It is shown that the statistical thermodynamic approach devised to explain the molecular origin of cold denaturation [G. Graziano, Phys. Chem. Chem. Phys., 2010, 12, 14245-14252] can provide a rationalization of the different behaviour of GdmCl and Gdm(2)SO(4) towar …
It is shown that the statistical thermodynamic approach devised to explain the molecular origin of cold denaturation [G. Graziano
On the mechanism of cold denaturation.
Graziano G. Graziano G. Phys Chem Chem Phys. 2014 Oct 21;16(39):21755-67. doi: 10.1039/c4cp02729a. Epub 2014 Sep 8. Phys Chem Chem Phys. 2014. PMID: 25198426
A theoretical rationalization of the occurrence of cold denaturation for globular proteins was devised, assuming that the effective size of water molecules depends upon temperature [G. Graziano, Phys. Chem. Chem. Phys., 2010, 12, 14245-14252]. In the present work, i …
A theoretical rationalization of the occurrence of cold denaturation for globular proteins was devised, assuming that the effective size of …
347 results