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N- and C-Terminal Truncations to Enhance Protein Solubility and Crystallization: Predicting Protein Domain Boundaries with Bioinformatics Tools.

Cooper, Christopher D.O. and Marsden, Brian D. (2017) N- and C-Terminal Truncations to Enhance Protein Solubility and Crystallization: Predicting Protein Domain Boundaries with Bioinformatics Tools. In: Heterologous Gene Expression in E.coli: Methods and Protocols. Methods in Molecular Biology, 1586 . Springer, pp. 11-31. ISBN 978-1493968879

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Abstract

Soluble protein expression is a key requirement for biochemical and structural biology approaches to study biological systems in vitro. Production of sufficient quantities may not always be achievable if proteins are poorly soluble which is frequently determined by physico-chemical parameters such as intrinsic disorder. It is well known that discrete protein domains often have a greater likelihood of high-level soluble expression and crystallizability. Determination of such protein domain boundaries can be challenging for novel proteins. Here, we outline the application of bioinformatics tools to facilitate the prediction of potential protein domain boundaries, which can then be used in designing expression construct boundaries for parallelized screening in a range of heterologous expression systems.

Item Type: Book Chapter
Uncontrolled Keywords: Truncations, Protein expression, Protein solubility, Protein structure, Domain, BLAST, PSIPRED, Hidden Markov Model (HMM), Alignment, Secondary structure
Subjects: Q Science > QR Microbiology
Schools: School of Applied Sciences
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Depositing User: Christopher Cooper
Date Deposited: 05 Jul 2017 08:49
Last Modified: 05 Jul 2017 18:30
URI: http://eprints.hud.ac.uk/id/eprint/32365

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