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1H{19F} NOE NMR Structural Signatures of the Insulin R6 Hexamer: Evidence of a Capped HisB10 Site in Aryl- and Arylacryloyl-carboxylate Complexes

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Abstract

New and improved insulin: 1H{19F} NOE NMR difference spectra for CF3-substituted aromatic carboxylates bound at the HisB10 sites of the R6 human insulin (HI) hexamer show strong NOEs between the CF3 groups and the LeuB6, AsnB3, and PheB1 sidechains. The NOEs and structural modeling establish that these carboxylates form closed complexes with the HisB10 site capped by the PheB1 rings.

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