Determinants of protein folding and aggregation in P22 tailspike protein

Matthew J Gage, Brian G. Lefebvre, Anne S. Robinson

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

The P22 tailspike protein is a well-studied model system for understanding multimeric protein folding and aggregation. It is one of the few systems for which both in vivo and in vitro folding pathways have been well characterized. Aggregation of the P22 tailspike occurs through a multimeric addition pathway in which both monomeric and multimeric protein can associate with existing aggregates promoting aggregate growth.

Original languageEnglish (US)
Title of host publicationMisbehaving Proteins: Protein (Mis)Folding, Aggregation, and Stability
PublisherSpringer New York
Pages247-264
Number of pages18
ISBN (Print)9780387360638, 0387305084, 9780387305080
DOIs
StatePublished - 2006

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ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Gage, M. J., Lefebvre, B. G., & Robinson, A. S. (2006). Determinants of protein folding and aggregation in P22 tailspike protein. In Misbehaving Proteins: Protein (Mis)Folding, Aggregation, and Stability (pp. 247-264). Springer New York. https://doi.org/10.1007/978-0-387-36063-8_11