Proteins, Enzymes

10:10 AM - 10:30 AM JST(1:10 AM - 1:30 AM UTC)

[3OA-03] Effect of phosphorylation on structures, dynamics, and properties of N-terminal domain of spider dragline silk proteins and its implications for spider silk synthesis

*Nur Alia Oktaviani¹, Hamish C Craig¹, Mami Goto¹, Keiji Numata^1,2 (1. Biomacromolecules research team, RIKEN Center for Sustainable Resource Sciences, 2. Department of Material Chemistry, Graduate School of Engineering, Kyoto University)

Keywords:

Post translational modifications (PTMs),spider silk protein,structure,dynamics,properties,N-terminal domain

Despite post translational modification (PTMs) playing a key role in functional proteomics, only little is known about PTMs on spider silk. In this study, we investigated the effect of phosphorylation on the structure dynamics and properties of NTD of spider dragline silk proteins. The effect of phosphorylation on NTD was elucidated by producing recombinant phosphomimic NTDs through the mutation of serine or threonine to aspartate.Our study shows that phosphomimic NTDs have similar structure and dynamics but different properties compared to the wildtypes. The insight of this study is useful to synthesize the artificial spider dragline silk with tunable properties.