Mutations and off-pathway aggregation of proteins

doi:10.1016/0167-7799(94)90082-5

Trends in Biotechnology

Volume 12, Issue 5, May 1994, Pages 193-198

https://doi.org/10.1016/0167-7799(94)90082-5 Get rights and content

Abstract

The off-pathway aggregation of proteins is a ubiquitous, yet poorly understood, phenomenon. In vitro, aggregation places limits on both protein stability and refolding yields. In vivo, it is responsible for inclusion-body formation in the bacterial production of proteins, as well as amyloid disease and related phenomena in animals. An important common feature of these processes is their sensitivity to point mutations, a feature that offers important clues for understanding controversial aspects of off-pathway aggregation such as its molecular specificity and the nature of the aggregating species. Results of a number of studies illustrate that the sensitivity of aggregation can derive from the ability of a mutation to either (1) facilitate the accumulation of a non-native state that is prone to aggregation, or (2) increase the intrinsic tendency of such a state to aggregate.

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Trends in Biotechnology

ReviewMutations and off-pathway aggregation of proteins

Abstract

Trends Biochem. Sci.

J. Biol. Chem.

J. Biol. Chem.

J. Biol. Chem.

J. Mol. Biol.

J. Biol. Chem.

Hemat. Oncol. Clin. N. Am.

J. Mol. Biol.

J. Physiol.

Science

Protein Eng.

Biochemistry

Protein Eng.

Bio/Technology

Eur. J. Biochem.

Angewandte Chemie (English)

Biochemistry

Biochemistry

Annu. Rev. Biochem.

Nature

Review
Mutations and off-pathway aggregation of proteins