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. 1972 Apr;69(4):975–979. doi: 10.1073/pnas.69.4.975

Study of Adrenocorticotropic Hormone Conformation by Evaluation of Intramolecular Resonance Energy Transfer in Nε-Dansyllysine21-ACTH-(1-24)-Tetrakosipeptide

Peter W Schiller 1,*
PMCID: PMC426607  PMID: 4337249

Abstract

The solution conformation of ACTH was studied by intramolecular resonance energy transfer and fluorescence depolarization with the synthetic, biologically active, derivative Nε-dansyllysine21-ACTH-(1-24)-tetrakosipeptide. The Förster parameters involved in energy transfer from the donor Trp9 to the dansyl acceptor attached to the side chain of Lys21 were determined from measurements with ACTH fragments containing either the donor or the acceptor alone. From determinations of the fluorescence quantum yields of the donor in the derivative and in the native ACTH-(1-24)-tetrakosipeptide, it was shown that besides energy transfer no additional quenching of the donor fluorescence is introduced by the presence of the acceptor. The short measured rotational relaxation time of the dansyl chromophore reflects the flexibility of the lysine side chain and justifies the use of an average value for the orientation factor in the distance calculations. The calculated intramolecular distance is remarkably independent of solvent, indicating a “random coil” situation with regard to residues 9-21.

Keywords: fluorescence spectra, Förster parameters, side-chain flexibility, intramolecular distances

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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