Evidence map›Paper›PMID 29487966›Full record

ArticleEuropean biophysics journal : EBJ2018

Mechanisms of antifreeze proteins investigated via the site-directed spin labeling technique.

Antonia Flores, Justin C Quon, Adiel F Perez, Yong Ba

Abstract read
In one paragraph

Article in European biophysics journal : EBJ, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Review
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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

4 authors.

Antonia FloresDepartment of Chemistry and Biochemistry, California State University, Los Angeles, 5151 State University Drive, Los Angeles, CA, 90032, USA.
Justin C QuonDepartment of Chemistry and Biochemistry, California State University, Los Angeles, 5151 State University Drive, Los Angeles, CA, 90032, USA.
Adiel F PerezDepartment of Chemistry and Biochemistry, California State University, Los Angeles, 5151 State University Drive, Los Angeles, CA, 90032, USA.
Yong BaDepartment of Chemistry and Biochemistry, California State University, Los Angeles, 5151 State University Drive, Los Angeles, CA, 90032, USA. yba@calstatela.edu.ORCID http://orcid.org/0000-0003-1079-4708

Funding

Research Initiative for Scientific Enhancement (RISE)R25GM061331 · NIGMS · CALIFORNIA STATE UNIVERSITY LOS ANGELES · PI FOSTER, KRISHNA L · 2000 to 2021
$33.1M
Spin Labeled Ice Binding Proteins for Molecular Antifreeze Mechanistic StudyR15GM106249 · NIGMS · CALIFORNIA STATE UNIVERSITY LOS ANGELES · PI BA, YONG · 2014 to 2014
$319k
NIGMS NIH HHS R15 GM106249NIGMS NIH HHS R25 GM061331NIH HHS R15GM106249
6 · The paper itself

Abstract

The site-directed spin labeling (SDSL) technique was used to examine the antifreeze mechanisms of type-I antifreeze proteins (AFPs). The effects on the growth of seed ice crystals by the spin-label groups attached to different side chains of the AFPs were observed, and the states of water molecules surrounding the spin-label groups were probed via analyses of variable-temperature (VT) dependent electron paramagnetic resonance (EPR) spectra. The first set of experiments revealed the antifreeze activities of the spin-labeled AFPs at the microscopic level, while the second set of experiments displayed those at the molecular level. The experimental results confirmed the putative ice-binding surface (IBS) of type-I AFPs. The VT EPR spectra indicate that type-I AFPs can inhibit the nucleation of seed ice crystals down to ~ - 20 °C in their aqueous solutions. Thus, the present authors believe that AFPs protect organisms from freezing damage in two ways: (1) inhibiting the nucleation of seed ice crystals, and (2) hindering the growth of seed ice crystals once they have formed. The first mechanism should play a more significant role in protecting against freezing damage among organisms living in cold environments. The VT EPR spectra also revealed that liquid-like water molecules existed around the spin-labeled non-ice-binding side chains of the AFPs frozen within the ice matrices, and ice surrounding the spin-label groups melted at subzero temperatures during the heating process. This manuscript concludes with the proposed model of antifreeze mechanisms of AFPs based on the experimental results.

Indexed as

Spin LabelsAntifreeze ProteinsBinding SitesElectron Spin Resonance SpectroscopyIceModels, MolecularMutationProtein ConformationAntifreeze ProteinsIceSpin LabelsIce crystalsIce growth inhibitionIce nucleation inhibitionSite-directed spin labelingType-I antifreeze proteinVT EPR

Identifiers

PMID29487966
PMCPMC6709975

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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.