Evidence map›Paper›PMID 29193968›Full record

ArticleJournal of the American Chemical Society2018

Structural Insight into the Photochemistry of Split Green Fluorescent Proteins: A Unique Role for a His-Tag.

Alan Deng, Steven G Boxer

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

18 citing papers in PubMed, 31 citations in OpenAlex.

  1. Tuning Polyacrylate Composition to Recognize and Modulate Fluorescent Proteins.Angewandte Chemie (International ed. in English) · 2026
    Article
  2. Review
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  5. DNA-Regulated Multi-Protein Complement Control.Journal of the American Chemical Society · 2024
    Article
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  14. Cell-type-specific, multicolor labeling of endogenous proteins with split fluorescent protein tags inProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  15. Article
  16. Review
  17. Article
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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

2 authors at 1 institution in 1 country.

Alan DengDepartment of Chemistry, Stanford University , Stanford, California 94305-5012, United States.ORCID 0000-0002-3893-7128
Steven G BoxerDepartment of Chemistry, Stanford University , Stanford, California 94305-5012, United States.ORCID 0000-0001-9167-4286
Stanford University · US

Funding

X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Biophysical Studies of Macromolecules and Molecular AssembliesR35GM118044 · NIGMS · STANFORD UNIVERSITY · PI STEVEN G. BOXER · 2016 to 2026
$7.2M
NMR &CIDNP STUDIES OF MB MUTANTS &OLIGONUCLEOTIDE LOOPR01GM027738 · NIGMS · STANFORD UNIVERSITY · PI BOXER, STEVEN G. · 1985 to 2016
$4.3M
ELECTROSTATICS AND DYNAMICS IN MYOGLOBIN MUTANTSR37GM027738 · NIGMS · STANFORD UNIVERSITY · PI BOXER, STEVEN G. · 1994 to 2003
$1.2M
NIGMS NIH HHS P41 GM103393NIGMS NIH HHS R01 GM027738NIGMS NIH HHS R35 GM118044NIGMS NIH HHS R37 GM027738
6 · The paper itself

Abstract

Oligohistidine affinity tags (His-tags) are commonly fused to proteins to aid in their purification via metal affinity chromatography. These His-tags are generally assumed to have minimal impact on the properties of the fusion protein, as they have no propensity to form ordered elements, and are small enough not to significantly affect the solubility or size. Here we report structures of two variants of truncated green fluorescent protein (GFP), i.e., split GFP with a β-strand removed, that were found to behave differently in the presence of light. In these structures, the N-terminal His-tag and several neighboring residues play a highly unusual structural and functional role in stabilizing the truncated GFP by substituting as a surrogate β-strand in the groove vacated by the native strand. This finding provides an explanation for the seemingly very different peptide binding and photodissociation properties of split proteins involving β-strands 10 and 11. We show that these truncated GFPs can bind other non-native sequences, and this promiscuity invites the possibility for rational design of sequences optimized for strand binding and photodissociation, both useful for optogenetic applications.

Indexed as

Photochemical ProcessesChromatography, AffinityGreen Fluorescent ProteinsHistidineLightMolecular StructureProtein Structure, SecondaryGreen Fluorescent ProteinsHistidine

Identifiers

PMID29193968
PMCPMC5815829
OpenAlexW2775798691

What OpenQuestion holds

Textmetadata
LicenceTDM
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.