Energy landscape in protein folding and unfolding

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

doi:10.1073/pnas.1524864113

Energy landscape in protein folding and unfolding

Journal Article · Tue Mar 08 00:00:00 EST 2016 · Proceedings of the National Academy of Sciences of the United States of America

DOI:https://doi.org/10.1073/pnas.1524864113· OSTI ID:1437126

Mallamace, Francesco ^[1]; Corsaro, Carmelo ^[2]; Mallamace, Domenico ^[3]; Vasi, Sebastiano ^[4]; Vasi, Cirino ^[5]; Baglioni, Piero ^[6]; Buldyrev, Sergey V. ^[7]; Chen, Sow -Hsin ^[8]; Stanley, H. Eugene ^[9]

CNR-Istituto per i Processi Chimico Fisici Messina, Messina (Italy); Massachusetts Inst. of Technology (MIT), Cambridge, MA (United States); Boston Univ., Boston, MA (United States); Boston University
CNR-Istituto per i Processi Chimico Fisici Messina, Messina (Italy); Univ. di Messina, Messina (Italy)
Consorzio per lo Sviluppo dei Sistemi a Grande Interfase, Catania (Italy)
Univ. di Messina, Messina (Italy)
CNR-Istituto per i Processi Chimico Fisici Messina, Messina (Italy)
Univ. di Firenze and Consorzio per lo Sviluppo dei Sistemi a Grande Interfase, Florence (Italy)
Yeshiva Univ., New York, NY (United States)
Massachusetts Inst. of Technology (MIT), Cambridge, MA (United States)
Boston Univ., Boston, MA (United States)

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. Here, 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.

View Accepted Manuscript (DOE)

Research Organization:: Massachusetts Inst. of Technology (MIT), Cambridge, MA (United States)

Sponsoring Organization:: USDOE

Grant/Contract Number:: FG02-90ER45429

OSTI ID:: 1437126

Journal Information:: Proceedings of the National Academy of Sciences of the United States of America, Journal Name: Proceedings of the National Academy of Sciences of the United States of America Journal Issue: 12 Vol. 113; ISSN 0027-8424

Publisher:: National Academy of Sciences, Washington, DC (United States)Copyright Statement

Country of Publication:: United States

Language:: English

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