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PMID: 1367308 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Predicting the solubility of recombinant proteins in Escherichia coli.

Bio/technology (Nature Publishing Company) ·Vol. 9 ·No. 5 ·1991-05-00 ·Pages 443-8

Wilkinson DL, Harrison RG

Abstract

We have studied the cause of inclusion body formation in Escherichia coli grown at 37 degrees C using statistical analysis of the composition of 81 proteins that do and do not form inclusion bodies. Six composition derived parameters were used. In declining order of their correlation with inclusion body formation, the parameters are charge average, turn forming residue fraction, cysteine fraction, proline fraction, hydrophilicity, and total number of residues. The correlation with inclusion body formation is strong for the first two parameters but weak for the last four. This correlation can be used to predict the probability that a protein will form inclusion bodies using only the protein's amino acid composition as the basis for the prediction.

MeSH Terms
Amino Acids/metabolism Animals Escherichia coli/genetics,metabolism Humans Models, Statistical Probability Recombinant Proteins/metabolism Solubility Temperature
Chemicals
Amino Acids Recombinant Proteins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Wilkinson D L
School of Chemical Engineering and Material Science, University of Oklahoma, Norman 73019.
Harrison R G
Article Info
Journal
Bio/technology (Nature Publishing Company)
Abbr.
Biotechnology (N Y)
ISSN
0733-222X
Published
1991-05-00
Pages
443-8
Language
English
Region
United States
NLM ID
8309273
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