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Cited by 122Protein Structure and DynamicsProtein purification and stabilityAdvanced NMR Techniques and Applications

Energy landscape in protein folding and unfolding

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Mallamace, Francesco, Corsaro, Carmelo, Mallamace, Domenico, Vasi, Sebastiano, Vasi, Cirino, Baglioni, Piero, Buldyrev, Sergey V., Chen, Sow-Hsin +1 more·2016·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.1524864113PMC PMC4812744
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Abstract

Significance: 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. 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.

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  • Protein folding exhibits irreversible fates and fitness landscapes, whereas irreversibility is rarely quantified in population genetics, where traditional models are fundamentally time reversible.

    “Like development, protein folding exhibits irreversible fates (184, 185) and fitness landscapes (186–189), whereas irreversibility is rarely quantified in population genetics, where traditional models are fundamentally time reversible (190).”

    From Topological Approaches in Animal Comparative Genomics (2026) · cites this paper as [185]

    In “Energy landscape in protein folding and unfolding” (page unavailable), the paper describes a free-energy landscape for protein folding and an irreversible denatured state. It does not describe that landscape as a fitness landscape; the citing sentence assigns the population-genetics comparison to a different citation. (LLM, conf=0.86)

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Research works printed but not linked: 33

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Authors
Mallamace, F., Corsaro, C., Mallamace, D., Vasi, S., Vasi, C., Baglioni, P., Buldyrev, S. V., Chen, S.-H., & Stanley, H. E.
Affiliations
  • Boston University (US)
  • University of Messina (IT)
  • Consorzio Interuniversitario per lo Sviluppo dei Sistemi a Grande Interfase (IT)
  • Institute for Chemical and Physical Processes (IT)
  • Yeshiva University (US)
  • Massachusetts Institute of Technology (US)
  • Center for Polymer Studies and Department of Physics, Boston University, Boston, MA 02215;
ORCID
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
2016-03-08
Volume
113
Issue
12
Pages
3159-3163
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.1524864113
PMC
PMC4812744
OpenAlex
W2296239589
Cited by
122
References
0
Citations by year
2026: 7 · 2025: 19 · 2024: 8 · 2023: 12 · 2022: 11 · 2021: 14 · 2020: 13 · 2019: 16 · 2018: 12 · 2017: 6 · 2016: 4
FWCI
5.41
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • Florence Research (University of Florence) (submittedVersion, other-oa)
  • OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
  • DSpace@MIT (Massachusetts Institute of Technology) (submittedVersion, cc-by-nc)
Funders
  • National Science Foundation (1505000, 1213217, 1125290, DE-FG02-90ER45429)
  • U.S. Department of Energy (DE‐FG02‐, FG02-90ER45429, DEFG0290ER45429)
  • Massachusetts Institute of Technology
  • Consiglio Nazionale delle Ricerche
  • Division of Civil, Mechanical and Manufacturing Innovation (1125290, CMMI-1125290)
  • Division of Chemistry (1213217)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
  • Physical Sciences › Chemistry › Spectroscopy › Advanced NMR Techniques and Applications
Keywords
protein folding, protein unfolding, free energy landscape, lysozyme, magnetization, hydration, native state, thermodynamic anomalies, water compressibility
MeSH terms
Muramidase, Protein Denaturation, Temperature, Protein Folding, Proton Magnetic Resonance Spectroscopy

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