Biochemical Journal · 1971 · 30 citations · 4 references
MedicineEndocrinologyPharmacologyBiopharmaceuticsClinical PharmacologyDiabetologyDiabetes MellitusDiabetes Mellitus BiochemistryDiabetes PharmacotherapyGlycemic ControlInsulin TherapyPancreatic HormonesHuman InsulinInsulin BiochemistryInsulin PharmacologyIntravenous Insulin TherapyLong-acting Insulin AnaloguesPubmed Search
The close juxtaposition of residues Al and B30 in the insulin structure shows that only a few residues of the rather long and species-variable connecting peptide of proinsulin are required to connect these groups. The position of residues Al and B30 on the surface of the hexamer is con- sistent with the reported dimerization and hexamer- ization of proinsulin.
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