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Title: Energy landscape in protein folding and unfolding

Abstract

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.

Authors:
 [1];  [2];  [3];  [4];  [5];  [6];  [7];  [8];  [9]
  1. 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)
  2. CNR-Istituto per i Processi Chimico Fisici Messina, Messina (Italy); Univ. di Messina, Messina (Italy)
  3. Consorzio per lo Sviluppo dei Sistemi a Grande Interfase, Catania (Italy)
  4. Univ. di Messina, Messina (Italy)
  5. CNR-Istituto per i Processi Chimico Fisici Messina, Messina (Italy)
  6. Univ. di Firenze and Consorzio per lo Sviluppo dei Sistemi a Grande Interfase, Florence (Italy)
  7. Yeshiva Univ., New York, NY (United States)
  8. Massachusetts Inst. of Technology (MIT), Cambridge, MA (United States)
  9. Boston Univ., Boston, MA (United States)
Publication Date:
Research Org.:
Massachusetts Inst. of Technology (MIT), Cambridge, MA (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1437126
Grant/Contract Number:  
FG02-90ER45429
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
Proceedings of the National Academy of Sciences of the United States of America
Additional Journal Information:
Journal Volume: 113; Journal Issue: 12; Journal ID: ISSN 0027-8424
Publisher:
National Academy of Sciences, Washington, DC (United States)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; protein folding; proton NMR; energy landscape; hydration water

Citation Formats

Mallamace, Francesco, Corsaro, Carmelo, Mallamace, Domenico, Vasi, Sebastiano, Vasi, Cirino, Baglioni, Piero, Buldyrev, Sergey V., Chen, Sow -Hsin, and Stanley, H. Eugene. Energy landscape in protein folding and unfolding. United States: N. p., 2016. Web. doi:10.1073/pnas.1524864113.
Mallamace, Francesco, Corsaro, Carmelo, Mallamace, Domenico, Vasi, Sebastiano, Vasi, Cirino, Baglioni, Piero, Buldyrev, Sergey V., Chen, Sow -Hsin, & Stanley, H. Eugene. Energy landscape in protein folding and unfolding. United States. doi:10.1073/pnas.1524864113.
Mallamace, Francesco, Corsaro, Carmelo, Mallamace, Domenico, Vasi, Sebastiano, Vasi, Cirino, Baglioni, Piero, Buldyrev, Sergey V., Chen, Sow -Hsin, and Stanley, H. Eugene. Tue . "Energy landscape in protein folding and unfolding". United States. doi:10.1073/pnas.1524864113. https://www.osti.gov/servlets/purl/1437126.
@article{osti_1437126,
title = {Energy landscape in protein folding and unfolding},
author = {Mallamace, Francesco and Corsaro, Carmelo and Mallamace, Domenico and Vasi, Sebastiano and Vasi, Cirino and Baglioni, Piero and Buldyrev, Sergey V. and Chen, Sow -Hsin and Stanley, H. Eugene},
abstractNote = {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.},
doi = {10.1073/pnas.1524864113},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
issn = {0027-8424},
number = 12,
volume = 113,
place = {United States},
year = {2016},
month = {3}
}

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Cited by: 12 works
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Works referenced in this record:

The Dynamic Energy Landscape of Dihydrofolate Reductase Catalysis
journal, September 2006

  • Boehr, D. D.; McElheny, D.; Dyson, H. J.
  • Science, Vol. 313, Issue 5793, p. 1638-1642
  • DOI: 10.1126/science.1130258