Being learning the applications of some advanced optical spectroscopy

Being a
chemistry student, an undergraduate course on biological sciences initially
introduced me to the central dogma of life, protein folding and biochemical
principles. The fundamental role biomolecules play in biological systems
inspired me to undertake a research project on protein chemistry. Through the
project, I got familiar with several new molecular biology techniques related
to recombinant protein expression, purification and characterization. Studying
protein-ligand interactions using biophysical methods was most exciting for me.
Over the course of the project, I developed a strong interest in molecular
biophysics especially in the use of spectroscopic techniques to probe
biomolecules. As spectroscopic measurements offer noninvasive and near
real-time method to study biological systems. Further, an introductory course
on quantum chemistry and spectroscopy provided me with the much required
theoretical background. 

Equipped with
some knowledge of spectroscopy, I am interested in learning the applications of
some advanced optical spectroscopy and microscopy techniques in protein
chemistry. Proteins are vital for the functioning of living organisms, but some
proteins undergo structural changes due to several factors giving rise to
diseases like Alzheimer, Parkinson and type II diabetes. One such protein is
the Amyloid Precursor Protein (APP), on proteolysis APP gives rise to Amyloid
Beta peptides which further undergoes aggregation. These amyloid plaques
disrupt the functioning of neuronal cells giving rise to Dementia and
Alzheimer’s disease. Aggregation of the amyloid beta-peptide into oligomers is a
vital process associated with the progression of Alzheimer’s disease.

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Small sized
amyloid beta oligomers are known to be more toxic than the large fibrils due to
their high affinity for biological membranes. Recent mutational studies have
highlighted the critical role of early non-local folding contact in the
toxicity of amyloid beta oligomers. But the conformational information for
membrane-bound and unbound states of small oligomers is limited. Hence, I am
interested in studying the conformations of membrane-bound small oligomers
using Surface Enhanced Raman Spectroscopy (SERS) to identify typical structural
features vital for the toxicity of amyloid beta oligomers. The method of
binding proteins to the lipid bilayer coated nanoparticles has opened up a new
avenue for studying protein conformations using SERS. In parallel, the
aggregation profile of amyloid beta can be monitored by Fluorescence
Correlation Spectroscopy (FCS) for a comparative study. So, using mainly SERS
and FCS, or other single molecule tools I would like to shed some light on the
conformations governing the toxicity of small amyloid beta oligomers.