By Daniel Herschlag
This MIE quantity offers laboratory concepts that objective to foretell the constitution of a protein which may have great implications starting from drug layout, to mobile pathways and their dynamics, to viral access into cells. professional researchers introduce the main complex applied sciences and strategies in protein constitution and foldingIncludes recommendations on tiling assays.
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Additional resources for Biophysical, Chemical, and Functional Probes of RNA Structure, Interactions and Folding:, Part 1
REFERENCES Adams, P. , Stahley, M. , Kosek, A. , Wang, J. , and Strobel, S. A. (2004). Crystal structure of a self-splicing group I intron with both exons. Nature 430, 45–50. , and Frey, P. A. (1994). A simplified procedure for synthesizing nucleoside 1-thiotriphosphates—dATPS, dGTPS, UTPS, and dTTPS. Biochem. Biophys. Res. Commun. 204, 150–155. , Rambo, R. , Cate, J. , Ferre-D’Amare, A. , Strobel, S. , and Doudna, J.
Revealed by the NAIM method, many of which are described below. Nucleotide analogs can be approximately classified into three groups: those deleting a functional group, those adding steric bulk to the functional group, and those altering the chemical nature of the functional group. Many analogs clearly modify more than one property of the nucleotide, so whenever possible a series of closely related analogs should be employed to dissect these effects. Nucleotide analog interference suppression (NAIS) has also been used to refine the role of functional groups at specific sites of interference (described below).
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