摘要
The studies of rhombohedral 2-zinc pig insulin crystal structure indicate that theN-terminal of B-chain is situated at molecular surface and has an extended conforma-tion which is arranged together with the neighboring residues A13 Leu, A14 Tyr inorder. In the structure model of insulin hexamer, these residues and the same res-idues in the neighboring dimer are close to each other, and they constitute the hydro-phobic interaction between the dimers. The variation in this region may directly af-fect the process of insulin hexamer forming and the crystalline features which
