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Insights into protein structure, stability and function from saturation mutagenesis

Gupta, Kritika and Varadarajan, Raghavan (2018) Insights into protein structure, stability and function from saturation mutagenesis. In: CURRENT OPINION IN STRUCTURAL BIOLOGY, 50 . pp. 117-125.

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Official URL: http://dx.doi.org/10.1016/j.sbi.2018.02.006


Where convenient phenotypic readouts are available, saturation mutagenesis coupled to deep sequencing provides a rapid and facile method to infer sequence determinants of protein structure, stability and function. We provide brief descriptions and currently available options for the various steps involved, and mention limitations of current implementations. We also highlight recent applications such as estimating relative stabilities and affinities of protein variants, mapping epitopes, protein model discrimination and prediction of mutant phenotypes. Most mutational scans have so far been applied to single genes and proteins. Additional methodological improvements are required to expand the scope to study intergenic epistasis and intermolecular interactions in macromolecular complexes.

Item Type: Journal Article
Additional Information: Copy right for this article belong to CURRENT BIOLOGY LTD, 84 THEOBALDS RD, LONDON WC1X 8RR, ENGLAND
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 25 Sep 2018 17:31
Last Modified: 25 Sep 2018 17:31
URI: http://eprints.iisc.ac.in/id/eprint/60718

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