PREDICTING THE SOLUBILITY OF RECOMBINANT PROTEINS IN ESCHERICHIA-COLI

被引：1

作者：

WILKINSON, DL ^{[1
]}

HARRISON, RG ^{[1
]}

机构：

[1] UNIV OKLAHOMA,SCH CHEM ENGN & MAT SCI,NORMAN,OK 73019

来源：

BIO-TECHNOLOGY | 1991年 / 9卷 / 05期

关键词：

D O I：

暂无

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

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.

引用

页码：443 / 448

页数：6

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