Evidence map›Paper›PMID 35313047›Full record

ArticleAngewandte Chemie (International ed. in English)2022

Cold Denaturation of Proteins in the Absence of Solvent: Implications for Protein Storage.

Emma L Norgate, Rosie Upton, Kjetil Hansen, Bruno Bellina, C Brookes, Argyris Politis, Perdita E Barran

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.2field-weighted citation impact, top 12% of its field
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

11 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
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  10. Cold Denaturation of Proteins in the Absence of Solvent: Implications for Protein Storage.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2022
    Article
  11. 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

7 authors at 3 institutions in 1 country.

Emma L NorgateManchester Institute of Biotechnology, University of Manchester, Princess Street, Manchester, M1 7DN, UK.
Rosie UptonManchester Institute of Biotechnology, University of Manchester, Princess Street, Manchester, M1 7DN, UK.
Kjetil HansenDepartment of Chemistry, King's College London, 7 Trinity Street, London, SE1 1DB, UK.
Bruno BellinaManchester Institute of Biotechnology, University of Manchester, Princess Street, Manchester, M1 7DN, UK.
C BrookesBristol-Myers Squibb, Moreton, Wirral, CH46 1QW, UK.
Argyris PolitisDepartment of Chemistry, King's College London, 7 Trinity Street, London, SE1 1DB, UK.
Perdita E BarranManchester Institute of Biotechnology, University of Manchester, Princess Street, Manchester, M1 7DN, UK.ORCID 0000-0002-7720-586X
University of Manchester · GBKing's College London · GBBristol-Myers Squibb (United Kingdom) · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L002655/1, BB/L016486/1 BB/M01108/1
6 · The paper itself

Abstract

The effect of temperature on the stability of proteins is well explored above 298 K, but harder to track experimentally below 273 K. Variable-temperature ion mobility mass spectrometry (VT IM-MS) allows us to measure the structure of molecules at sub-ambient temperatures. Here we monitor conformational changes that occur to two isotypes of monoclonal antibodies (mAbs) on cooling by measuring their collision cross sections (CCS) at discrete drift gas temperatures from 295 to 160 K. The CCS at 250 K is larger than predicted from collisional theory and experimental data at 295 K. This restructure is attributed to change in the strength of stabilizing intermolecular interactions. Below 250 K the CCS of the mAbs increases in line with prediction implying no rearrangement. Comparing data from isotypes suggest disulfide bridging influences thermal structural rearrangement. These findings indicate that in vacuo deep-freezing minimizes denaturation and maintains the native fold and VT IM-MS measurements at sub ambient temperatures provide new insights to the phenomenon of cold denaturation.

Indexed as

Cold TemperatureProteinsIon Mobility SpectrometryProtein DenaturationSolventsTemperatureProteinsSolventsCold DenaturationMonoclonal AntibodiesProtein FoldingStructure-Activity RelationshipsVariable-Temperature Ion Mobility

Identifiers

PMID35313047
PMCPMC9325448
OpenAlexW4220990644

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.