Evidence map›Paper›PMID 35914130›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

In vitro investigation of protein assembly by combined microscopy and infrared spectroscopy at the nanometer scale.

Xiao Zhao, Dong Li, Yi-Hsien Lu, Behzad Rad, Chunsheng Yan, Hans A Bechtel, Paul D Ashby, Miquel B Salmeron

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
  2. Article
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  5. Article
  6. Two-dimensional silk.Science advances · 2024
    Article
  7. Article
  8. Probing both sides of the story.Proceedings of the National Academy of Sciences of the United States of America · 2022
    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

8 authors.

Xiao ZhaoDepartment of Materials Science and Engineering, University of California at Berkeley, Berkeley, CA 94720.ORCID 0000-0003-1079-664X
Dong LiMolecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720.
Yi-Hsien LuMaterials Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720.
Behzad RadMolecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720.ORCID 0000-0001-6531-9168
Chunsheng YanMolecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720.
Hans A BechtelAdvanced Light Source, Lawrence Berkeley National Laboratory, Berkeley, CA 94720.
Paul D AshbyMolecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720.ORCID 0000-0003-4195-310X
Miquel B SalmeronDepartment of Materials Science and Engineering, University of California at Berkeley, Berkeley, CA 94720.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The nanoscale structure and dynamics of proteins on surfaces has been extensively studied using various imaging techniques, such as transmission electron microscopy and atomic force microscopy (AFM) in liquid environments. These powerful imaging techniques, however, can potentially damage or perturb delicate biological material and do not provide chemical information, which prevents a fundamental understanding of the dynamic processes underlying their evolution under physiological conditions. Here, we use a platform developed in our laboratory that enables acquisition of infrared (IR) spectroscopy and AFM images of biological material in physiological liquids with nanometer resolution in a cell closed by atomically thin graphene membranes transparent to IR photons. In this work, we studied the self-assembly process of S-layer proteins at the graphene-aqueous solution interface. The graphene acts also as the membrane separating the solution containing the proteins and Ca

Indexed as

Membrane GlycoproteinsMicroscopy, Atomic ForceNanotechnologySpectrophotometry, InfraredAmidesCalciumGraphiteOsmolar ConcentrationPhotonsSolventsWaterAmidesCalciumGraphiteMembrane GlycoproteinsS-layer proteinsSolventsWaternano-FTIRoperando spectroscopyself-assemblyS-layer proteinsolid-liquid interface

Identifiers

PMID35914130
PMCPMC9371722

What OpenQuestion holds

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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.