A role of disordered domains in regulating protein oligomerization and stability

Ofrah Faust; Lavi Bigman; Assaf Friedler

doi:10.1039/c4cc03863k

A role of disordered domains in regulating protein oligomerization and stability

Ofrah Faust
, Lavi Bigman
, Assaf Friedler^*

^*Corresponding author for this work

Institute of Chemistry

Research output: Contribution to journal › Article › peer-review

12 Scopus citations

Abstract

Intrinsically disordered proteins (IDPs) or regions (IDRs) in proteins hold many functions but their biological roles are still not fully understood. Here we describe a new role of such regions. Using the HIV-1 Rev protein, we show that disordered domains have a role in maintaining the correct oligomeric state and the thermodynamic stability of proteins.

Original language	English
Pages (from-to)	10797-10800
Number of pages	4
Journal	Chemical Communications
Volume	50
Issue number	74
DOIs	https://doi.org/10.1039/c4cc03863k
State	Published - 18 Aug 2014

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10.1039/c4cc03863k

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abstract = "Intrinsically disordered proteins (IDPs) or regions (IDRs) in proteins hold many functions but their biological roles are still not fully understood. Here we describe a new role of such regions. Using the HIV-1 Rev protein, we show that disordered domains have a role in maintaining the correct oligomeric state and the thermodynamic stability of proteins.",

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AB - Intrinsically disordered proteins (IDPs) or regions (IDRs) in proteins hold many functions but their biological roles are still not fully understood. Here we describe a new role of such regions. Using the HIV-1 Rev protein, we show that disordered domains have a role in maintaining the correct oligomeric state and the thermodynamic stability of proteins.

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A role of disordered domains in regulating protein oligomerization and stability

Abstract

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