Evidence map›Paper›PMID 38527099›Full record

ArticleThe journal of physical chemistry letters2024

Dynamical Transition in Dehydrated Proteins.

Johanna Kölbel, Moritz L Anuschek, Ivonne Stelzl, Supawan Santitewagun, Wolfgang Friess, J Axel Zeitler

Abstract read
In one paragraph

Article in The journal of physical chemistry letters, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

6 authors.

Johanna KölbelDepartment of Chemical Engineering, University of Cambridge, Cambridge CB3 0AS, U.K.
Moritz L AnuschekDepartment of Chemical Engineering, University of Cambridge, Cambridge CB3 0AS, U.K.
Ivonne StelzlDepartment of Pharmacy - Center for Drug Research, Pharmaceutical Technology and Biopharmaceutics, Ludwig-Maximilians Universität, Butenandtstrasse 5, 81377 Munich, Germany.
Supawan SantitewagunDepartment of Chemical Engineering, University of Cambridge, Cambridge CB3 0AS, U.K.
Wolfgang FriessDepartment of Pharmacy - Center for Drug Research, Pharmaceutical Technology and Biopharmaceutics, Ludwig-Maximilians Universität, Butenandtstrasse 5, 81377 Munich, Germany.
J Axel ZeitlerDepartment of Chemical Engineering, University of Cambridge, Cambridge CB3 0AS, U.K.ORCID 0000-0002-4958-0582

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Terahertz time-domain spectroscopy and differential scanning calorimetry were used to study the role of the dynamics of biomolecules decoupled from solvent effects. Lyophilized sucrose exhibited steadily increasing absorption with temperature as anharmonic excitations commenced as the system emerged from a deep minimum of the potential energy landscape where harmonic vibrations dominate. The polypeptide bacitracin and two globular proteins, lysozyme and human serum albumin, showed a more complex temperature dependence. Further analysis focused on the spectral signature below and above the boson peak. We found evidence of the onset of anharmonic motions that are characteristic for partial unfolding and molecular jamming in the dry biomolecules. The activation of modes of the protein molecules at temperatures comparable to the protein dynamical transition temperature was observed in the absence of hydration. No evidence of Fröhlich coherence, postulated to facilitate biological function, was found in our experiments.

Indexed as

ProteinsWaterHumansSolventsTemperatureProteinsSolventsWater

Identifiers

PMID38527099
PMCPMC11000241

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Registered trials

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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.