Evidence map›Paper›PMID 9655345›Full record

ArticleProtein science : a publication of the Protein Society1998

From coiled coils to small globular proteins: design of a native-like three-helix bundle.

J W Bryson, J R Desjarlais, T M Handel, W F DeGrado

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

53 citing papers in PubMed, 136 citations in OpenAlex.

  1. Chemical science · 2025
    Article
  2. Article
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  4. Article
  5. Catalysis and Electron Transfer inChemical reviews · 2022
    Review
  6. Nitrite reductase activity within an antiparallel de novo scaffold.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021
    Article
  7. Review
  8. Article
  9. Modulation of a protein-folding landscape revealed by AFM-based force spectroscopy notwithstanding instrumental limitations.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Article
  11. Article
  12. Quarterly reviews of biophysics · 2020
    Review
  13. Rational De Novo Design of a Cu Metalloenzyme for Superoxide Dismutation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020
    Article
  14. Article
  15. MinimalistACS catalysis · 2019
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  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

4 authors at 4 institutions in 1 country.

J W BrysonThe DuPont Merck Pharmaceutical Company, Wilmington, Delaware, USA.
J R Desjarlais
T M Handel
W F DeGrado
Johnson Foundation · USUniversity of California, Berkeley · USUniversity of Pennsylvania · USWilmington University · US

Funding

De novo design of alpha-helical bundlesR37GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 2004 to 2013
$3.6M
DE NOVO DESIGN OF ALPHA HELICAL BUNDLESR01GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 1996 to 2016
$2.4M
NIGMS NIH HHS GM54616
6 · The paper itself

Abstract

A monomolecular native-like three-helix bundle has been designed in an iterative process, beginning with a peptide that noncooperatively assembled into an antiparallel three-helix bundle. Three versions of the protein were designed in which specific interactions were incrementally added. The hydrodynamic and spectroscopic properties of the proteins were examined by size exclusion chromatography, sedimentation equilibrium, fluorescence spectroscopy, and NMR. The thermodynamics of folding were evaluated by monitoring the thermal and guanidine-induced unfolding transitions using far UV circular dichroism spectroscopy. The attainment of a unique, native-like state was achieved through the introduction of: (1) helix capping interactions; (2) electrostatic interactions between partially exposed charged residues; (3) a diverse collection of apolar side chains within the hydrophobic core.

Indexed as

Protein ConformationProtein Structure, SecondaryAmino Acid SequenceChemical PhenomenaChemistry, PhysicalChromatography, GelDeuteriumDimerizationDrug DesignElectrochemistryHot TemperatureMacromolecular SubstancesMagnetic Resonance SpectroscopyModels, MolecularMolecular Sequence DataMolecular WeightDeuteriumMacromolecular SubstancesPeptides

Identifiers

PMID9655345
PMCPMC2144029
OpenAlexW2007606609

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.