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Study · Not a test of the peptide alone · 1990

3 results

Solution conformation of thymosin beta 4: a nuclear magnetic resonance and simulated annealing study.

Zarbock J, Oschkinat H, Hannappel E, Kalbacher H, Voelter W, Holak TA

Biochemistry1 Aug 1990Cited by 62 (Europe PMC)

PMID2261438 (opens in a new tab)DOI10.1021/bi00486a006 (opens in a new tab)PepBankPUB-02261438
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 study3

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

Studies that did not test the peptide alone3

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)Other

    In trifluoroethanol and hexafluoroisopropyl alcohol solutions, NMR structure calculations showed two helical regions in thymosin beta‑4, at residues 4-16 and 30-40.

    In plain wordsIn lab tests in alcohol-water solutions, thymosin beta‑4 formed two helical regions. This is a structure result only.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableHelical regions of Tβ4 in solution
    Study

    n: not reported in source

    Tβ4 in trifluoroethanol or hexafluoroisopropyl alcohol solution
    Outcome group
    Peptide structure and chemistry · Pharmacology

    Measurements

    helical region residues
    4 to 16 residues
    first helix
    helical region residues
    30 to 40 residues
    second helix

    Source sentences

    Summary
    Analysis of the 30 converged structures indicates that there are two helical regions extending from residues 4-16 and from residues 30-40, which are well defined both in terms of atomic root mean square differences and backbone torsion angles.
    1 context sentence
    Summary · context
    The conformation of the polypeptide thymosin beta 4 in solutions of 60% (v/v) trifluoroethanol-d3 and 50% (v/v) hexafluoroisopropyl-d2 alcohol in water is investigated by nuclear magnetic resonance (NMR) spectroscopy.

    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)Other

    In the 30 calculated structures, the average backbone rms difference between pairs of structures within each of the two helical regions was approximately 2 A.

    In plain wordsIn lab tests, the calculated structures of the two helical regions of thymosin beta‑4 agreed closely with each other.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableBackbone rms difference within helical regions
    Study

    n: not reported in source

    Tβ4 in trifluoroethanol or hexafluoroisopropyl alcohol solution
    Outcome group
    Peptide structure and chemistry · Pharmacology

    Measurements

    average backbone rms difference
    ≈ 2 A
    helical regions

    Source sentences

    Summary
    For the two helical regions individually the average backbone rms difference between all pairs of structures is approximately 2 A.
    1 context sentence
    Summary · context
    The conformation of the polypeptide thymosin beta 4 in solutions of 60% (v/v) trifluoroethanol-d3 and 50% (v/v) hexafluoroisopropyl-d2 alcohol in water is investigated by nuclear magnetic resonance (NMR) spectroscopy.

    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).

  3. 03LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Other

    All 30 calculated structures of thymosin beta‑4 satisfied the experimental NMR constraints and had small deviations from idealized covalent geometry.

    In plain wordsIn lab tests, all 30 calculated structures of thymosin beta‑4 fitted the NMR measurements.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableAgreement of calculated structures with NMR constraints
    Study

    n: not reported in source

    Tβ4 in trifluoroethanol or hexafluoroisopropyl alcohol solution
    Outcome group
    Peptide structure and chemistry · Pharmacology

    Measurements

    calculated structures
    30 structures
    all satisfy constraints

    Source sentences

    Summary
    All 30 calculated structures satisfy the experimental constraints, display very small deviations from idealized covalent geometry, and possess good nonbonded contacts.
    1 context sentence
    Summary · context
    The conformation of the polypeptide thymosin beta 4 in solutions of 60% (v/v) trifluoroethanol-d3 and 50% (v/v) hexafluoroisopropyl-d2 alcohol in water is investigated by nuclear magnetic resonance (NMR) spectroscopy.

    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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