Abstract
Structural information about proteins can provide valuable insight into folding mechanisms and dynamics, giving us information about protein function and interactions within biological systems. Upon interaction with various moieties, proteins have the potential to undergo a variety of conformational changes. Extensive studies have been done using deep UV resonance Raman (dUVRR) spectroscopy to study the secondary structure of proteins. Here, we present the results of our experiments, where we simultaneously monitored both secondary and tertiary structure of de novo synthesized protein, HP7.
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