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N27: Physics of Proteins: Folding and Function

101H

Sponsoring Units: DBIOChair: Wouter Hoff, Oklahoma State University-StillwaterSession Tags:
  • Focus

Wed. March 6, 12:18 p.m. – 12:30 p.m. CST

101H

The rapid aggregation of misfolded proteins leads to various neurodegenerative diseases. Beta-amyloid and tau protein are two proteins associated with Alzheimer's disease. Studies have shown that Raman spectroscopy can reveal important information about protein structures, including misfolding or denaturing processes. Using a Raman microscope with an excitation laser at 532 nm, we studied the vibrational spectrum of different protein aggregations among various stages of fibrillations as a function of temperature, from 20°C to 200°C. Our results show changes in the proteins’ Raman signatures as part of the heating process. Our study demonstrates a label-free and non-destructive technique to investigate amyloid fibril formation and study their secondary and tertiary structure as a function of temperature.  Such data could, one day, enable the design of novel photothermal treatments for Alzheimer's disease.

 

 




 



 



 


 


Presented By

  • Yin-Ting Yeh (National Standard of Institute and technology)

Authors

  • Yin-Ting Yeh (National Standard of Institute and technology)
  • Thuc Mai (National Institute of Standards and Technology)
  • Angela R Hight Walker (National Institute of Standards and Tech)