Graziano G - Search Results

1

A Rationalization of the Effect That TMAO, Glycine, and Betaine Exert on the Collapse of Elastin-like Polypeptides.

Pica A, Graziano G. Pica A, et al. Among authors: graziano g. Life (Basel). 2022 Jan 18;12(2):140. doi: 10.3390/life12020140. Life (Basel). 2022. PMID: 35207427 Free PMC article.

2

Exploring the unfolding mechanism of γ-glutamyltranspeptidases: the case of the thermophilic enzyme from Geobacillus thermodenitrificans.

Pica A, Russo Krauss I, Castellano I, Rossi M, La Cara F, Graziano G, Sica F, Merlino A. Pica A, et al. Among authors: graziano g. Biochim Biophys Acta. 2012 Apr;1824(4):571-7. doi: 10.1016/j.bbapap.2012.01.014. Epub 2012 Jan 31. Biochim Biophys Acta. 2012. PMID: 22322192

3

Effect of NaCl on the conformational stability of the thermophilic γ-glutamyltranspeptidase from Geobacillus thermodenitrificans: Implication for globular protein halotolerance.

Pica A, Russo Krauss I, Castellano I, La Cara F, Graziano G, Sica F, Merlino A. Pica A, et al. Among authors: graziano g. Biochim Biophys Acta. 2013 Jan;1834(1):149-57. doi: 10.1016/j.bbapap.2012.09.014. Epub 2012 Oct 2. Biochim Biophys Acta. 2013. PMID: 23036908

4

On the Effect of Sodium Chloride and Sodium Sulfate on Cold Denaturation.

Pica A, Graziano G. Pica A, et al. Among authors: graziano g. PLoS One. 2015 Jul 21;10(7):e0133550. doi: 10.1371/journal.pone.0133550. eCollection 2015. PLoS One. 2015. PMID: 26197394 Free PMC article.

5

On the effect of sodium salts on the coil-to-globule transition of poly(N-isopropylacrylamide).

Pica A, Graziano G. Pica A, et al. Among authors: graziano g. Phys Chem Chem Phys. 2015 Nov 7;17(41):27750-7. doi: 10.1039/c5cp04094a. Phys Chem Chem Phys. 2015. PMID: 26435490

Since this phenomenon resembles the cold renaturation of globular proteins, it can be studied by means of the theoretical approach devised to rationalise the occurrence and the mechanism of cold denaturation [G. Graziano, Phys. Chem. Chem. Phys., 2010, 12, 14245; Ph …

Since this phenomenon resembles the cold renaturation of globular proteins, it can be studied by means of the theoretical approach devised t …

6

On urea's ability to stabilize the globule state of poly(N-isopropylacrylamide).

Pica A, Graziano G. Pica A, et al. Among authors: graziano g. Phys Chem Chem Phys. 2016 Jun 7;18(21):14426-33. doi: 10.1039/c5cp07507f. Epub 2016 May 12. Phys Chem Chem Phys. 2016. PMID: 27171496

7

Shedding light on the extra thermal stability of thermophilic proteins.

Pica A, Graziano G. Pica A, et al. Among authors: graziano g. Biopolymers. 2016 Dec;105(12):856-63. doi: 10.1002/bip.22923. Biopolymers. 2016. PMID: 27449333 Review.

8

An alternative explanation of the cononsolvency of poly(N-isopropylacrylamide) in water-methanol solutions.

Pica A, Graziano G. Pica A, et al. Among authors: graziano g. Phys Chem Chem Phys. 2016 Sep 14;18(36):25601-25608. doi: 10.1039/c6cp04753j. Phys Chem Chem Phys. 2016. PMID: 27722309

9

Hydrostatic pressure effect on PNIPAM cononsolvency in water-methanol solutions.

Pica A, Graziano G. Pica A, et al. Among authors: graziano g. Biophys Chem. 2017 Dec;231:34-38. doi: 10.1016/j.bpc.2017.01.001. Epub 2017 Jan 5. Biophys Chem. 2017. PMID: 28081859

10

Comment on "Relating side chain organization of PNIPAm with its conformation in aqueous methanol" by D. Mukherji, M. Wagner, M. D. Watson, S. Winzen, T. E. de Oliveira, C. M. Marques and K. Kremer, Soft Matter, 2016, 12, 7995.

Pica A, Graziano G. Pica A, et al. Among authors: graziano g. Soft Matter. 2017 Nov 1;13(42):7698-7700. doi: 10.1039/c7sm01065f. Soft Matter. 2017. PMID: 29051960

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