Prediction of some spatial structures of proinsulin by hydropathic mass

Title:Prediction of some spatial structures of proinsulin by hydropathic mass

Volume: 7 Issue: 3

Author(s): Rong-Qiao HE*, Yang Liu and Ying Liu

Affiliation:

• Lab Visual Information Processing, Institute of Biophysics, The Chinese Academy of Sciences, 15 Da Tun Rd, Chaoyang District, Beijing 100101, China

Abstract: Hydropathic mass (HM) has been used to display the characterization of hydrophilicity and hydrophobicity of proinsulin. The a-helix of the B chain (residues 9-19), which is located at the inner part of the crystalline insulin, possesses a strong positive HM. The proteolytic sites of proinsulin for insulin maturation are located in the most negative HM regions. This suggests that they are exposed to the exterior of the molecule, which contributes to the digestion by proteases during insulin maturing.

Cite this article as:

Rong-Qiao HE *, Liu Yang and Liu Ying, Prediction of some spatial structures of proinsulin by hydropathic mass, Protein & Peptide Letters 2000; 7 (3) . https://dx.doi.org/10.2174/092986650703221206123247