Elucidating protein structure

In normal, or off-resonance Raman scattering the incident photon at a frequency outside of any electronic absorption band is inelastically scattered, leaving the molecule in an excited vibrational level of the electronic ground state (for Stokes scattering).A similar vibrational transition occurs for resonance Raman scattering, where excitation occurs at a frequency within an electronic absorption band.An understanding of the encoded protein folding “rules” would dramatically speed insight into protein structure and function.A number of mechanisms have been proposed that differ in the order of folding events.However, these static x-ray structures do not give the dynamic structural information essential to determine enzymatic mechanisms, for example.Nuclear magnetic resonance spectroscopy (NMR) is an extraordinarily powerful tool for studying protein folding.

In addition, UVRR studies of sidechain vibrations will probe the role of side chains in determining protein secondary, tertiary and quaternary structures.Unfortunately, the use of IR absorption spectroscopy is challenging for biological samples, because it is generally limited to DO.Raman spectroscopy is an inelastic light scattering phenomenon where the incident electromagnetic field interacts with a molecule such that there is an exchange of a quantum of vibrational energy between the two, resulting in a vibrational frequency difference between the incident and scattered light.The framework model propose the occurrence of funnel-shaped folding energy landscapes, where the native state is accessed via a strategically sloped energy landscape that funnel myriads of partially folded conformations towards the native folded state.Numerous experimental techniques are being applied to study protein folding.

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