N- and C-terminal truncations to enhance protein solubility and crystallization: Predicting protein domain boundaries with bioinformatics tools

Christopher D.O. Cooper, Brian D. Marsden

Research output: Chapter in Book/Report/Conference proceedingChapter

3 Citations (Scopus)

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.

Original languageEnglish
Title of host publicationHeterologous Gene Expression in E.coli
Subtitle of host publicationMethods and Protocols
EditorsNicola A. Burgess-Brown
PublisherHumana Press Inc.
Pages11-31
Number of pages21
ISBN (Electronic)9781493968879
ISBN (Print)9781493968855
DOIs
Publication statusPublished - 4 May 2017

Publication series

NameMethods in Molecular Biology
Volume1586
ISSN (Print)1064-3745

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    Cooper, C. D. O., & Marsden, B. D. (2017). N- and C-terminal truncations to enhance protein solubility and crystallization: Predicting protein domain boundaries with bioinformatics tools. In N. A. Burgess-Brown (Ed.), Heterologous Gene Expression in E.coli: Methods and Protocols (pp. 11-31). (Methods in Molecular Biology; Vol. 1586). Humana Press Inc.. https://doi.org/10.1007/978-1-4939-6887-9_2