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Orientation of the tryptophanyl side chain in [(d)TrpA1] and [TrpA1]insulin

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Abstract

Insulin analogues withl- andd-tryptophan instead of glycine in A1 permit an estimate of the proximity relationship between the indole residue of tryptophan and B19-tyrosine by evaluation of singlet-singlet resonance energy transfer. A significantly higher transfer efficiency is observed with [(d)TrpA1]insulin than with the [TrpA1]analogue. On the basis of this result it is possible to deduce the arrangement of the side chains and the α-amino groups in position A1 of [(d)TrpA1] and [TrpA1]insulin.

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Schiller, P.W., Geiger, R. Orientation of the tryptophanyl side chain in [(d)TrpA1] and [TrpA1]insulin. J Protein Chem 2, 279–287 (1983). https://doi.org/10.1007/BF01025594

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  • DOI: https://doi.org/10.1007/BF01025594

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