Isolation of viral coat protein mutants with altered assembly and aggregation properties.

doi:10.1093/nar/29.22.e113

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Article

Isolation of viral coat protein mutants with altered assembly and aggregation properties.

Nucleic acids research - 15 Nov 2001

Peabody D S, Al-Bitar L

Abstract excerpt

A method was developed to screen bacteria for synthesis of mutant proteins with altered assembly and solubility properties using bacteriophage MS2 coat protein as a model self-associating protein. Colonies expressing coat protein from a plasmid were covered with an agarose overlay under conditions that caused the lysis of some of the cells in each colony. The proteins thus liberated diffused through the overlay...

Topics

Amino Acid Substitution
Bacteriophage T7
Capsid
Capsid Proteins
Dimerization
Electrophoresis, Agar Gel
Electrophoresis, Polyacrylamide Gel
Escherichia coli
Genetic Vectors
Models, Molecular
Molecular Structure
Mutation
Promoter Regions, Genetic
Protein Conformation
RNA-Binding Proteins
Solubility

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Identifiers

PMID: 11713333
DOI: 10.1093/nar/29.22.e113
PMCID: PMC92581

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