Spectral Fluctuation Raman Spectroscopy (SFRS)

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Brief Description

       Our ability to experimentally measure the biomacromolecular structure of proteins and their complexes down to the atomic scale has progressed at a staggering pace in recent years. However, the dynamical conformational changes that affect, to name a few examples, DNA transcription, energy-transfer in photosynthesis and enzyme activity, and the transition from healthy to diseased states, remain difficult to capture. A non-perturbative, label-free approach that is sensitive to individual conformational states is single-protein Raman spectroscopy. However, the time resolution of single-protein Raman spectroscopy is typically limited to milliseconds (10^-3 sec), limited by inherent signal strength. Protein conformational dynamics occur over a timescale ranging from tens of seconds down to microseconds (10^-6 sec) or even nanoseconds (10^-9 sec).

      To address these challenges UC Berkeley researchers have developed a novel, high-temporal dynamic range Raman spectrometer capable of measuring sub-microsecond, and even nanosecond, fluctuations in single- and few-molecule spectra. The available dynamic range can be used to study and control of biomolecular dynamics as related to protein-protein interactions, drug discovery, validating computational biophysics capabilities, and many other additional applications. 

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