Structural Order in the Hydration Shell of Nonpolar Groups versus that in Bulk Water
G Graziano - ChemPhysChem, 2024 - Wiley Online Library
The poor solubility of nonpolar compounds in water around room temperature is governed
by a large and negative entropy change, whose molecular cause is still debated. Since the …
by a large and negative entropy change, whose molecular cause is still debated. Since the …
Destabilization of the D2 domain of Thermotoga maritima arginine binding protein induced by guanidinium thiocyanate and its counteraction by stabilizing agents
G Izzi, A Paladino, R Oliva, G Barra, A Ruggiero… - Protein …, 2024 - Wiley Online Library
D2 is a structural and cooperative domain of Thermotoga maritima Arginine Binding Protein,
that possesses a remarkable conformational stability, with a denaturation temperature of …
that possesses a remarkable conformational stability, with a denaturation temperature of …
[HTML][HTML] Entropy-driven polymer collapse on increasing the temperature: The case of poly (N-vinylcaprolactam)
G Graziano - Journal of Molecular Liquids, 2024 - Elsevier
Abstract Poly (N-vinylcaprolactam), PNVCL, chains undergo a temperature-induced,
reversible and endothermic collapse in water at around 32° C. The entropy gain driving …
reversible and endothermic collapse in water at around 32° C. The entropy gain driving …
[HTML][HTML] Is Water the Engine of Protein Folding?
M Campanile, G Graziano - Biophysica, 2024 - mdpi.com
No one can dismiss the fundamental role played by water in several important biochemical
processes, including the folding of globular proteins. The so-called hydrophobic effect is the …
processes, including the folding of globular proteins. The so-called hydrophobic effect is the …