Work

Energy landscape in protein folding and unfolding

Year: 2016

Type: article

Abstract: Significance Protein folding represents an open question in science, and the free-energy landscape framework is one way to describe it. In particular, the role played by water in the processes is of special interest. To clarify these issues we study, during folding–unfolding, the temperature evolution of the magnetization for hydrophilic and hydrophobic groups of hydrated lysozyme using NMR spectroscopy. Our findings confirm the validity of the theoretical scenario of a process dominated by different energetic routes, also explaining the water role in the protein configuration stability. We also highlight that the protein native state limit is represented by the water singular temperature that characterizes its compressibility and expansivity and is the origin of the thermodynamical anomalies of its liquid state.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.1524864113

Authors: Francesco Mallamace, Carmelo Corsaro, Domenico Mallamace, Sebastiano Vasi, Cirino Vasi, Piero Baglioni, Sergey V. Buldyrev, Sow-Hsin Chen, H. Eugene Stanley

Institutions: Boston University, Institute for Chemical and Physical Processes, Massachusetts Institute of Technology, University of Messina, Consorzio Interuniversitario per lo Sviluppo dei Sistemi a Grande Interfase, University of Florence, Yeshiva University

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funders: National Science Foundation, U.S. Department of Energy, Massachusetts Institute of Technology, Consiglio Nazionale delle Ricerche, Division of Civil, Mechanical and Manufacturing Innovation, Division of Chemistry

Awards: G222768804, G2619044695, Collaborative Research: Unraveling Cerebral Connectivity with Diffusion MRI, Microscopy and Statistical Physics, CONSTRUCTION OF A SMALL ANGLE NEUTRON SCATTERING SPECTROMETER FOR INVESTIGATION OF MICROEMULSIONS AND NUCLEAR SOLUTIONS IN BULK IN POROUS, Collaborative Reseach: Ordering Process in Water, Aqueous Solutions, and Water-Biomolecule Systems, CDI-Type II: Collaborative Research: Dynamical processes in interdependent techno-social networks, NEUTRON AND X-RAY SCATTERING STUDIES OF THE LIQUID-LIQUID TRANSITION IN SUPERCOOLED CONFINED WATER.., G702394665, G7241185112, G7520120651

OpenAlex ID: W2296239589

FWCI: 4.967

Cites: 39

Cited by: 122

Related to: 10