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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. https://doi.org/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. 2016. "Energy landscape in protein folding and unfolding". United States. https://doi.org/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},
url = {https://www.osti.gov/biblio/1437126}, 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 = {Tue Mar 08 00:00:00 EST 2016},
month = {Tue Mar 08 00:00:00 EST 2016}
}

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Cited by: 72 works
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journal, August 2011


Supercooled liquids, glass transitions, and the Kauzmann paradox
journal, June 1988


The influence of water on protein properties
journal, October 2014


 -Helix folding in the presence of structural constraints
journal, July 2008


Transport properties of glass-forming liquids suggest that dynamic crossover temperature is as important as the glass transition temperature
journal, December 2010


Levinthal's paradox.
journal, January 1992


Negative activation enthalpies in the kinetics of protein folding.
journal, September 1995


The middle way
journal, January 2000


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


Water-inserted alpha-helical segments implicate reverse turns as folding intermediates
journal, June 1989


Navigating the folding routes
journal, March 1995


Water Mediation in Protein Folding and Molecular Recognition
journal, June 2006


Works referencing / citing this record:

Influence of glycerol on the cooling effect of pair hydrophobicity in water: relevance to proteins’ stabilization at low temperature
journal, January 2019


Quantum Approach to Fast Protein-Folding Time *
journal, August 2019


The Role of Hydrogen Bonding in the Folding/Unfolding Process of Hydrated Lysozyme: A Review of Recent NMR and FTIR Results
journal, November 2018


Crystal elasto-plasticity on the Poincaré half-plane
journal, July 2020


Unfolding and Refolding of Protein by a Combination of Ionic and Nonionic Surfactants
journal, July 2018


Genuine antiplasticizing effect of water on a glass-former drug
journal, August 2017


Alpha-Synuclein is a Target of Fic-mediated Adenylylation/AMPylation: Implications for Parkinson's Disease
journal, January 2019


Glutamine Hydrolysis by Imidazole Glycerol Phosphate Synthase Displays Temperature Dependent Allosteric Activation
journal, February 2018


The Role of Hydrogen Bonding in the Folding/Unfolding Process of Hydrated Lysozyme: A Review of Recent NMR and FTIR Results
journal, November 2018