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Updated: May 8, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
09:25

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

本質的に乱れたタンパク質のダイナミクスは,潜在的にシードアグリゲーションの種となるような,メタスタブルな形状を明らかにする

Qin Qiao1, Gregory R Bowman, Xuhui Huang

  • 1Bioengineering Graduate Program, Division of Biomedical Engineering, ‡Department of Chemistry, §Center of Systems Biology and Human Health, School of Science and Institute for Advance Study, The Hong Kong University of Science and Technology , Clear Water Bay, Kowloon, Hong Kong.

Journal of the American Chemical Society
|September 12, 2013
PubMed
まとめ

人間のアミリン (hIAPP) アグリゲーションは,II型糖尿病と関連しています. この研究は,集積核形成とβ細胞死を理解するために不可欠なhIAPPモノメアの変態状態を明らかにしています.

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