Energy landscape in protein folding and unfolding
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Mallamace-2016-Energy landscape in.pdf
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Author(s)
Mallamace, Francesco
Corsaro, Carmelo
Mallamace, Domenico
Vasi, Sebastiano
Vasi, Cirino
Baglioni, Piero
Buldyrev, Sergey V.
Chen, Sow-Hsin
Stanley, H. Eugene
Date Issued
December 2015
Journal
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences (U.S.)
Citation
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.” Proceedings of the National Academy of Sciences 113, no. 12 (March 2016): 3159–3163 © 2016 National Academy of Sciences
Version
Final published version
Abstract
We use 1H NMR to probe the energy landscape in the protein folding and unfolding process. Using the scheme ⇄ reversible unfolded (intermediate) → irreversible unfolded (denatured) state, we study the thermal denaturation of hydrated lysozyme that occurs when the temperature is increased. Using thermal cycles in the range 295
MIT Department
Massachusetts Institute of Technology. Department of Nuclear Science and Engineering
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Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
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DOI of Published Version
https://doi.org/10.1073/pnas.1524864113
