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Study · Not a test of the peptide alone · 2000

2 results

Structural requirements for thymosin beta4 in its contact with actin. An NMR-analysis of thymosin beta4 mutants in solution and correlation with their biological activity.

Simenel C, Van Troys M, Vandekerckhove J, Ampe C, Delepierre M

European journal of biochemistry1 Jun 2000Cited by 23 (Europe PMC)

PMID10848969 (opens in a new tab)DOI10.1046/j.1432-1327.2000.01380.x (opens in a new tab)PepBankPUB-10848969
Publisher pagePubMedAsk about this study
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Summary

The text of this summary is not shown here, because the article license does not allow reuse. Read it at the source (opens in a new tab)

Text rights: Publisher copyright. Results still quote short attributed sentences.

Results from this study2

No result from this study comes from a test of the peptide.

Studies that did not test the peptide alone2

In this study, Thymosin beta-4 (human) was a lab tool or a carrier, part of a mix, or the subject of a lab method. These results are not evidence about taking Thymosin beta-4 (human).

  1. 01LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Mechanism

    By NMR in 60% trifluoroethanol, wild-type thymosin beta4 formed an alpha-helix at residues 5-16 and a second alpha-helix at residues 31-39.

    In plain wordsIn lab tests, thymosin beta4 formed two helix-shaped regions in a solvent.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableWild-type thymosin beta4 conformation by NMR
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Pharmacology

    Measurements

    Helix I residues
    5 to 16 residues
    wild-type thymosin beta4
    Helix II residues
    31 to 39 residues
    wild-type thymosin beta4

    Source sentences

    Summary
    the wild-type thymosin beta4 conformation consists of an alpha-helix (helix I) extending from residues 5-16 with a more stable fragment from lysine 11 to lysine 16 and a second alpha-helix (helix II) encompassing residues 31-39.
    1 context sentence
    Summary · context
    We examined the conformational preferences of mutants of thymosin beta4, an actin monomer sequestering protein by NMR spectroscopy in 60% (v/v) trifluoroethanol.

    In this study, Thymosin beta-4 (human) was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Thymosin beta-4 (human).

  2. 02LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Activity measurement

    In thymosin beta4 mutants, extension of helix I at its C-terminal end over the LKK-segment resulted in loss of activity.

    In plain wordsIn lab tests, thymosin beta4 mutants with a longer helix lost activity.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    DecreaseActivity of thymosin beta4 mutants with extended helix I
    Study

    n: not reported in source

    Comparator
    Wild-type thymosin beta4
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    We determine that an extension of helix I at its C-terminal end over the LKK-segment results in loss of activity.
    1 context sentence
    Summary · context
    We examined the conformational preferences of mutants of thymosin beta4, an actin monomer sequestering protein by NMR spectroscopy in 60% (v/v) trifluoroethanol.

    In this study, Thymosin beta-4 (human) was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Thymosin beta-4 (human).

AI wrote and checked these results. AI can make mistakes, so check important results against the source.

Version history

PepBank keeps every version of the data on this study. Status changes from Retraction Watch, Europe PMC and Crossref are listed with their source.

  1. Version 2Current

    13 Oct 2026, 01:52 UTC

    Study results updated

  2. Version 1

    12 Oct 2026, 18:17 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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