A Survey of the Current Drug Screening Techniques to Obtain Rational Design and Study Drug -Target Interactions

Abstract
Different techniques have been developed over the years for the purpose of studying proteins
and understanding their functions. Early techniques typically employed bioluminescence or
fluorescence such such as the firefly protein luciferase and the jellyfish green fluorescent protein
(GFP), respectively, to localize proteins within the cell. X-ray crystallography has also provided
valuable structural details of many different proteins in vitro. Yet, nuclear magnetic resonance (NMR)
spectroscopy offers the most realistic insight into proteins' physiologic structures and how proteins
function in their native, cellular environments.
In-cell NMR spectroscopy is a technique that can exploit the nuclei of proteins in order to
discern their structures and binding interactions in atomic resolution. This requires use of a chemical
shift library or reference spectrum respectively, to which the chemical shifts of the protein under
study can be compared. The results offer real time analys

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