Evidence map›Paper›PMID 28413816›Full record

ArticleData in brief2017

Spectroscopic and AFM characterization of polypeptide-surface interactions: Controls and lipid quantitative analyses.

Øyvind Strømland, Ørjan S Handegård, Morten L Govasli, Hanzhen Wen, Samuel Furse, Øyvind Halskau

Open access · goldAbstract read
In one paragraph

Article in Data in brief, 2017. 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
0.2field-weighted citation impact, top 45% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  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 at 1 institution in 1 country.

Øyvind StrømlandDepartment of Molecular Biology, University of Bergen, Bergen, Norway.
Ørjan S HandegårdDepartment of Molecular Biology, University of Bergen, Bergen, Norway.
Morten L GovasliDepartment of Molecular Biology, University of Bergen, Bergen, Norway.
Hanzhen WenDepartment of Molecular Biology, University of Bergen, Bergen, Norway.
Samuel FurseDepartment of Molecular Biology, University of Bergen, Bergen, Norway.
Øyvind HalskauDepartment of Molecular Biology, University of Bergen, Bergen, Norway.
University of Bergen · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This article is related to http://dx.doi.org/10.1016/j.bbamem.2017.01.005 (Ø. Strømland, Ø.S. Handegård, M.L. Govasli, H. Wen, Ø. Halskau, 2017) [1]. In protein and polypeptide-membrane interaction studies, negatively charged lipids are often used as they are a known driver for membrane interaction. When using fluorescence spectroscopy and CD as indicators of polypeptide binding and conformational change, respectively, the effect of zwitterionic lipids only should be documented. The present data documents several aspects of how two engineered polypeptides (A-Cage-C and A-Lnk-C) derived from the membrane associating protein alpha-Lactalbumin affects and are affected by the presence of zwitterionic bilayers in the form of vesicles. We here document the behavior or the Cage and Lnk segments with respect to membrane interaction and their residual fold, using intrinsic tryptophan fluorescence assays. This data description also documents the coverage of solid-supported bilayers prepared by spin-coating mica using binary lipid mixes, a necessary step to ensure that AFM is performed on areas that are covered by lipid bilayers when performing experiments. Uncovered patches are detectable by both force curve measurements and height measurements. We tested naked mica׳s ability to cause aggregation as seen by AFM, and found this to be low compared to preparations containing negatively charged lipids. Work with lipids also carries the risk of chemical degradation taking place during vesicles preparation or other handling of the lipids. We therefor use

Indexed as

AFM, Atomic Force MicroscopyANTS, 8-Aminonaphthalene-1,3,6-Trisulfonic Acid Disodium SaltCD, Circular DichroismChemical degradationCircular dichroismCUBO solvent, Culeddu-Bosco solventDLS, Dynamic Light ScatteringDPX, p-Xylene-Bis-Pyridinium BromideEYPC, egg yolk phosphatidylcholineFluorescenceFRET, Förster Resonance Energy TransferLipid bilayersLUV, Large Unilamellar VesiclesNMR, Nuclear Magnetic ResonancePA, Phosphatidic AcidPBPS, porcine brain phosphatidylserinePC, PhosphatidylcholinePC-plas, Phosphatidylcholine plasmalogenPolypeptide aggregationPS, PhosphatidylserinePS-plas, Phosphatidylserine plasmalogenQuantitiative 31P NMRSLB, Solid-supported Lipid Bilayers.Solid-supported bilayersSpin-coating

Identifiers

PMID28413816
PMCPMC5384297
OpenAlexW2594338799

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.