Energy landscape in protein folding and unfolding
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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<T<365 K and following different trajectories along the protein energy surface, we observe that the hydrophilic (the amide NH) and hydrophobic (methyl CH3 and methine CH) peptide groups evolve and exhibit different behaviors. We also discuss the role of water and hydrogen bonding in the protein configurational stability.
Date issued
2015-12Department
Massachusetts Institute of Technology. Department of Nuclear Science and EngineeringJournal
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
ISSN
0027-8424
1091-6490