Decrease of α-helix potential and biological activity of β-endorphin in response to modifications of Met5

L. Gráf, M. Hollósi, András Patthy, Ilona Berzétei, A. Rónai

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Correlation is demonstrated between the α-helix content in trifluoroethanol and the biological activity of some β-endorphin analogs modified in position 5. It is suggested that Met5 in the β-endorphin structure may participate in stabilizing the biologically active conformation of the molecule.

Original languageEnglish
Pages (from-to)47-51
Number of pages5
JournalNeuropeptides
Volume1
Issue number1
DOIs
Publication statusPublished - 1980

Fingerprint

Endorphins
Bioactivity
Trifluoroethanol
Conformations
Molecules

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology
  • Endocrinology, Diabetes and Metabolism
  • Clinical Neurology
  • Neuroscience(all)
  • Cellular and Molecular Neuroscience

Cite this

Decrease of α-helix potential and biological activity of β-endorphin in response to modifications of Met5. / Gráf, L.; Hollósi, M.; Patthy, András; Berzétei, Ilona; Rónai, A.

In: Neuropeptides, Vol. 1, No. 1, 1980, p. 47-51.

Research output: Contribution to journalArticle

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AU - Berzétei, Ilona

AU - Rónai, A.

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Y1 - 1980

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