Conformational Ensemble of B Chain in T_{6} Human Insulin Based on the Landau Free Energy

• Authors: Yanlin Lei , Jianfeng He , Jiaojiao Liu , Jing Li
• Languages of publication: EN

Abstracts

EN

Insulin is an important peptide hormone for the glucose metabolism. The structural flexibility of insulin B chain attracts a lot of our attention for understanding the biological activity. Our work carried out the extensive sampling to statistically clarify the structural changes of isolated T_{6} human insulin B chain. We introduced the Landau free energy to describe the isolated insulin B chain whose experimental structure locates a local energy minimum. Its trained model was subjected to thousands of heating and cooling circles between the high and low temperatures. Six typical structure clusters were found by classifying the final generated structures with RMSD and radius of gyration. The structures in clusters indicate the potential deformations of insulin B chain at residues 5-8 of N-terminus, residues 9-12 of central helix and residues 24-29 of C-terminus, which agrees with the experimental results.

Keywords

EN

insulin; structural flexibility; free energy; conformational ensemble

• Publisher: Institute of Physics, Polish Academy of Sciences
• Journal: Acta Physica Polonica A
• Year: 2018
• Volume: 133
• Issue: 5
• Pages: 1261-1265

Dates

published

2018-05

received

2017-10-04

(unknown)

2017-10-21

Contributors

author

Yanlin Lei

• School of Physics, Beijing Institute of Technology, Beijing 100081, P.R. China

author

Jianfeng He

• School of Physics, Beijing Institute of Technology, Beijing 100081, P.R. China

author

Jiaojiao Liu

• School of Physics, Beijing Institute of Technology, Beijing 100081, P.R. China

author

Jing Li

• Beijing Genetech Pharmaceutical Co. Ltd., Beijing 102299, P.R. China

Identifiers

DOI

10.12693/APhysPolA.133.1261