Session 1B: Symposium on “100 years of Raman Spectroscopy – Lab to Life”

Understanding Protein Folding Using Raman Spectroscopy

Proteins are complex three-dimensional structures vital for almost every biological process. It is the characteristic 3-D shape which imparts their specific biological activity. Even small changes in the environment of proteins can lead to protein misfolding. A misfolded protein is not only biologically inactive but may also impose serious health complications as well. Many misfolded proteins are associated with life- threatening diseases such as Alzheimer’s, Parkinson’s, Huntington’s diseases, etc. To reduce the events of misfolding, understanding the mechanism of protein folding is very important. Misfolded proteins undergo structural alterations that cause them to lose their function through different stages. Examining these partially unfolded protein states is key to understanding the protein folding mechanism. Despite various techniques, the protein folding process remains enigmatic. Raman spectroscopy provides valuable insights into protein structure and changes in conformation. By analyzing Raman spectra, we can differentiate between secondary structures such as helices and beta-sheets, as well as identify specific amino acid residues like tyrosine and tryptophan. In our investigation, we compared bovine serum albumin (BSA) proteins based on their distinct sequences and structures. Although determining a protein's complete structure from a Raman spectrum is challenging, Raman spectroscopy can detect subtle alterations in proteins, such as BSA, during melting. Our research underscores the importance of advancements in Raman spectroscopy for unravelling the complexities of proteins.