Evidence map›Paper›PMID 17822714›Full record

ArticleJournal of molecular biology2007

The rough energy landscape of superfolder GFP is linked to the chromophore.

Benjamin T Andrews, Andrea R Schoenfish, Melinda Roy, Geoffrey Waldo, Patricia A Jennings

Abstract read
In one paragraph

Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Biochemical and functional characterization ofFrontiers in microbiology · 2022
    Article
  5. Characterization of Fluorescent Proteins with Intramolecular Photostabilization*.Chembiochem : a European journal of chemical biology · 2021
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Peculiarities of the Super-Folder GFP Folding in a Crowded Milieu.International journal of molecular sciences · 2016
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

5 authors.

Benjamin T AndrewsDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, 92093-0375, USA.
Andrea R Schoenfish
Melinda Roy
Geoffrey Waldo
Patricia A Jennings

Funding

Project# 4: INTERACTIONS OF ANCHORING PROTEINS WITH THEIR TARGETSP01DK054441 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TAYLOR, SUSAN S. · 1999 to 2017
$27.3M
MOLECULAR BIOPHYSICS TRAINING PROGRAMT32GM008326 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KOMIVES, ELIZABETH A. · 1989 to 2020
$7.5M
Investigation of the Functional/Folding Landscapes of the Il-1 FamilyR01GM054038 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI JENNINGS, PATRICIA A · 2002 to 2010
$2.4M
FOLDING MECHANISM OF A BETA PROTEINR29GM054038 · NIGMS · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI JENNINGS, PATRICIA A · 1996 to 2000
$106k
NIDDK NIH HHS DK 54441NIDDK NIH HHS P01 DK054441NIGMS NIH HHS GM 08326NIGMS NIH HHS GM 54038NIGMS NIH HHS R01 GM054038NIGMS NIH HHS R29 GM054038NIGMS NIH HHS T32 GM008326
6 · The paper itself

Abstract

Many green fluorescent protein (GFP) variants have been developed for use as fluorescent tags, and recently a superfolder GFP (sfGFP) has been developed as a robust folding reporter. This new variant shows increased stability and improved folding kinetics, as well as 100% recovery of native protein after denaturation. Here, we characterize sfGFP, and find that this variant exhibits hysteresis as unfolding and refolding equilibrium titration curves are non-coincident even after equilibration for more than eight half-lives as estimated from kinetic unfolding and refolding studies. This hysteresis is attributed to trapping in a native-like intermediate state. Mutational studies directed towards inhibiting chromophore formation indicate that the novel backbone cyclization is responsible for the hysteresis observed in equilibrium titrations of sfGFP. Slow equilibration and the presence of intermediates imply a rough landscape. However, de novo folding in the absence of the chromophore is dominated by a smoother energy landscape than that sampled during unfolding and refolding of the post-translationally modified polypeptide.

Indexed as

ThermodynamicsCircular DichroismCyclophilin AFluorescent DyesGreen Fluorescent ProteinsGuanidineKineticsNuclear Magnetic Resonance, BiomolecularProtein ConformationProtein DenaturationProtein FoldingSpectrometry, FluorescenceCyclophilin AFluorescent DyesGreen Fluorescent ProteinsGuanidine

Identifiers

PMID17822714
PMCPMC2695656

What OpenQuestion holds

Textmetadata
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.