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2018 | 133 | 5 | 1261-1265
Article title

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

Content
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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.
Publisher

Year
Volume
133
Issue
5
Pages
1261-1265
Physical description
Dates
published
2018-05
received
2017-10-04
(unknown)
2017-10-21
Contributors
author
  • School of Physics, Beijing Institute of Technology, Beijing 100081, P.R. China
author
  • School of Physics, Beijing Institute of Technology, Beijing 100081, P.R. China
author
  • School of Physics, Beijing Institute of Technology, Beijing 100081, P.R. China
author
  • Beijing Genetech Pharmaceutical Co. Ltd., Beijing 102299, P.R. China
References
Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-appv133n5p21
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