Giuseppe Graziano

Full Professor of Physical Chemistry

University of Sannio

Italy

Research Interests

Explore related searches

Professors in Italy

Contact this professor

Get a free first email built on one of their papers, ready for you to edit and send yourself.

About

Giuseppe Graziano is a Full Professor of Physical Chemistry at the University of Sannio, Italy. His research interests encompass enthalpy-entropy compensation in aqueous solutions, protein folding dynamics, and the interactions of thiocyanate with peptides. He has contributed significantly to understanding solvation thermodynamics and the role of water in various biochemical processes, as evidenced by his recent publications.

Articles (18)

Year:

2025

Year:

2025

Year:

2024

Year:

2024

Year:

2024

Year:

2024

Year:

2024

Year:

2024

Year:

2023

Year:

2023

Year:

2022

Year:

2022

Year:

2022

Year:

2022

Year:

2021

Year:

2021

Year:

2021

Year:

2020

Collaborators (2)

Serena Cozzolino

KTH Royal Institute of Technology

SWEDEN

View details

Orlando Crescenzi

University of Naples Federico II

ITALY

View details

ApplyKite TwinLearns as you apply

Make your next move.

Prepare your application

Review drafts before you send them.

Giuseppe Graziano

Research Interests

Explore related searches

Contact this professor

About

Articles (18)

On Enthalpy–Entropy Compensation Characterizing Processes in Aqueous Solution

Remarks on Life Feasibility on the Red Planet

The interaction of thiocyanate with peptides—A computational study

On the Stabilizing Effect of Aspartate and Glutamate and Its Counteraction by Common Denaturants

A van der Waals Model of Solvation Thermodynamics

Structural Order in the Hydration Shell of Nonpolar Groups versus that in Bulk Water

Molecular-Scale Liquid Density Fluctuations and Cavity Thermodynamics

Is Water the Engine of Protein Folding?

The Action of Chemical Denaturants: From Globular to Intrinsically Disordered Proteins

The Relevance of Cavity Creation for Several Phenomena Occurring in Water

A Structure-Based Mechanism for the Denaturing Action of Urea, Guanidinium Ion and Thiocyanate Ion

On the Molecular Driving Force of Protein–Protein Association

Some Clues about Enzymes from Psychrophilic Microorganisms

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

General Counteraction Exerted by Sugars against Denaturants

Comment on “The Gibbs free energy of cavity formation in a diverse set of solvents”[J. Chem. Phys. 153, 134501 (2020)]

N-methylacetamide is a solvent better than water for amino acid side chains: A rationalization grounded in the solvent-excluded volume effect

Is water a good solvent for the denatured state of globular proteins?

Collaborators (2)

Serena Cozzolino

Orlando Crescenzi

Make your next move.