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

Institute of Chemistry

The Hebrew University of Jerusalem

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

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

All Science Journal Classification (ASJC) codes

Electronic, Optical and Magnetic Materials
General Chemistry
Ceramics and Composites
Metals and Alloys
Materials Chemistry
Surfaces, Coatings and Films
Catalysis

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This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1039/c4cc03863k

Cite this

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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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AU - Bigman, Lavi

AU - Friedler, Assaf

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N2 - 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.

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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U2 - 10.1039/c4cc03863k

DO - 10.1039/c4cc03863k

M3 - مقالة

C2 - 25054624

SN - 1359-7345

VL - 50

SP - 10797

EP - 10800

JO - Chemical Communications

JF - Chemical Communications

IS - 74

ER -

A role of disordered domains in regulating protein oligomerization and stability

Abstract

All Science Journal Classification (ASJC) codes

UN SDGs

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