Evidence map›Paper›PMID 8732752›Full record

ArticleProtein science : a publication of the Protein Society1996

Probing the tertiary structure of proteins by limited proteolysis and mass spectrometry: the case of Minibody.

F Zappacosta, A Pessi, E Bianchi, S Venturini, M Sollazzo, A Tramontano, G Marino, P Pucci

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Article
  3. Protein Structural Analysis via Mass Spectrometry-Based Proteomics.Advances in experimental medicine and biology · 2016
    Review
  4. Article
  5. Article
  6. Structure-specific ribonucleases for MS-based elucidation of higher-order RNA structure.Journal of the American Society for Mass Spectrometry · 2014
    Article
  7. Review
  8. Article
  9. On the relevance of the Met-turn methionine in metzincins.The Journal of biological chemistry · 2010
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Topological investigation of amyloid fibrils obtained from beta2-microglobulin.Protein science : a publication of the Protein Society · 2002
    Article
  17. The effect of prime-site occupancy on the hepatitis C virus NS3 protease structure.Protein science : a publication of the Protein Society · 2002
    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

8 authors.

F ZappacostaServizio di Spettrometria di Massa del CNR, Napoli, Italy.
A Pessi
E Bianchi
S Venturini
M Sollazzo
A Tramontano
G Marino
P Pucci

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A strategy that combines limited proteolysis experiments and mass spectrometric analysis of the fragments generated has been developed to probe protease-accessible sites on the protein surface. This integrated approach has been employed to investigate the tertiary structure of the Minibody, a de novo designed 64-residue protein consisting of a beta-sheet scaffold based on the heavy-chain variable-domain structure of a mouse immunoglobulin and containing two segments corresponding to the hypervariable H1 and H2 regions. The low solubility of the protein prevented a detailed characterization by NMR and/or X-ray. Different proteases were used under strictly controlled conditions and the cleavage sites were mapped onto the anticipated Minibody model, leading to the identification of the most exposed regions. A single-residue mutant was constructed and characterized, following the same procedure, showing a slightly higher correspondence with the predicted model. This strategy can be used to effectively supplement NMR and X-ray investigations of protein tertiary structure, where these procedures cannot provide definitive data, or to verify and refine protein models.

Indexed as

Protein Structure, TertiaryAmino Acid SequenceAnimalsAntibodies, MonoclonalCarrier ProteinsCrystallography, X-RayEndopeptidasesImmunoglobulinsMagnetic Resonance SpectroscopyMass SpectrometryMiceModels, MolecularMolecular Sequence DataPoint MutationAntibodies, MonoclonalCarrier ProteinsEndopeptidasesImmunoglobulinsMinibody (WT)

Identifiers

PMID8732752
PMCPMC2143402

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.