Evidence map›Paper›PMID 26957601›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Energy landscape in protein folding and unfolding.

Francesco Mallamace, Carmelo Corsaro, Domenico Mallamace, Sebastiano Vasi, Cirino Vasi, Piero Baglioni, Sergey V Buldyrev, Sow-Hsin Chen, H Eugene Stanley

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

24 citing papers in PubMed.

  1. Sequence-encoded dynamics diversify allostery within a conserved protein scaffold.Protein science : a publication of the Protein Society · 2026
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  10. The Hydrophobic Effect Studied by Using Interacting Colloidal Suspensions.International journal of molecular sciences · 2023
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Francesco MallamaceCNR-Istituto per i Processi Chimico Fisici Messina, I-98166 Messina, Italy; Department of Nuclear Science and Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139; Center for Polymer Studies and Department of Physics, Boston University, Boston, MA 02215; francesco.mallamace@unime.it hes@bu.edu.
Carmelo CorsaroCNR-Istituto per i Processi Chimico Fisici Messina, I-98166 Messina, Italy; Dipartimento di Fisica e di Scienze della Terra, Università di Messina, I-98166 Messina, Italy;
Domenico MallamaceConsorzio per lo Sviluppo dei Sistemi a Grande Interfase, Unità di Catania, I-95125 Catania, Italy;
Sebastiano VasiDipartimento di Fisica e di Scienze della Terra, Università di Messina, I-98166 Messina, Italy;
Cirino VasiCNR-Istituto per i Processi Chimico Fisici Messina, I-98166 Messina, Italy;
Piero BaglioniDipartimento di Chimica, Università di Firenze and Consorzio per lo Sviluppo dei Sistemi a Grande Interfase, I-50019 Florence, Italy;
Sergey V BuldyrevDepartment of Physics, Yeshiva University, New York, NY 10033.
Sow-Hsin ChenDepartment of Nuclear Science and Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139;
H Eugene StanleyCenter for Polymer Studies and Department of Physics, Boston University, Boston, MA 02215; francesco.mallamace@unime.it hes@bu.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We use (1)H 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.

Indexed as

Protein FoldingMuramidaseProtein DenaturationProton Magnetic Resonance SpectroscopyTemperatureMuramidaseenergy landscapehydration waterprotein foldingproton NMR

Identifiers

PMID26957601
PMCPMC4812744

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.