Insights to Human γD-Crystallin Unfolding by NMR Spectroscopy and Molecular Dynamics Simulations

Shu Shun Hsueh, Steven S.S. Wang, Shu Han Chen, Chia Lin Wang, Josephine W. Wu*, Ta Hsien Lin

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Human γD-crystallin (HGDC) is an abundant lens protein residing in the nucleus of the human lens. Aggregation of this and other structural proteins within the lens leads to the development of cataract. Much has been explored on the stability and aggregation of HGDC and where detailed investigation at the atomic resolution was needed, the X-ray structure was used as an initial starting conformer for molecular modeling. In this study, we implemented NMR-solution HGDC structures as starting conformers for molecular dynamics simulations to provide the missing pieces of the puzzle on the very early stages of HGDC unfolding leading up to the domain swap theories proposed by past studies. The high-resolution details of the conformational dynamics also revealed additional insights to possible early intervention for cataractogenesis.

Original languageEnglish
Article number1591
JournalInternational Journal Of Molecular Sciences
Issue number3
StatePublished - 1 Feb 2022


  • Aggregation
  • Cataract
  • Human γD-crystallin
  • Molecular dynamics simulations
  • NMR spectroscopy
  • Stability
  • Unfolding


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