Binding of intrinsically disordered proteins is not necessarily accompanied by a structural transition to a folded form.

Binding of intrinsically disordered proteins is not necessarily accompanied by a structural transition to a folded form. Research Abstract Details 

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Binding of intrinsically disordered proteins is not necessarily accompanied by a structural transition to a folded form. Abstract Text:

Alexander B Sigalov,Anastasia V Zhuravleva,Vladislav Yu Orekhov,

There are a large number of protein domains and even entire proteins, lacking ordered structure under physiological conditions. Intriguingly, a highly flexible, random coil-like conformation is the native and functional state for many proteins known to be involved in cell signaling. An example is a key component of immune signaling, the cytoplasmic region of the T cell receptor zeta subunit. This domain exhibits specific dimerization that is distinct from non-specific aggregation behavior seen in many systems. In this work, we use diffusion and chemical shift mapping NMR data to show that the protein does not undergo a transition between disordered and ordered states upon dimerization. This finding opposes the generally accepted view on the behavior of intrinsically disordered proteins, provides evidence for the existence of specific dimerization interactions for intrinsically disordered protein species and opens a new line of research in this new and quickly developing field.

Binding of intrinsically disordered proteins is not necessarily accompanied by a structural transition to a folded form. Publishing Authors By Initials

AB Sigalov,AV Zhuravleva,VY Orekhov,

For similar proteins research abstracts see: proteins research

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Binding of intrinsically disordered proteins is not necessarily accompanied by a structural transition to a folded form. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Biochimie

VOLUME: 89

Page Numbers: 419-21

Journal Abbreviation: Biochimie

ISSN: 0300-9084

DAY: 22

MONTH: 11

YEAR: 2006

Binding of intrinsically disordered proteins is not necessarily accompanied by a structural transition to a folded form. Information

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LANGUAGE: eng

NlmUniqueID: 1264604

Binding of intrinsically disordered proteins is not necessarily accompanied by a structural transition to a folded form. Keywords Mesh Terms:

KEYWORDS: Proteins

MESH TERMS: chemistry

Chemical & Substance for Abstract: Binding of intrinsically disordered proteins is not necessarily accompanied by a structural transition to a folded form. Information

Substance Name: Proteins

Registry Number: 0

Grant and Affiliation Information for Binding of intrinsically disordered proteins is not necessarily accompanied by a structural transition to a folded form.

AFFILIATION: Department of Pathology, University of Massachusetts Medical School, Worcester, MA 01655, USA. alexander.sigalov@umassmed.edu

Country: France

AGENCY: United States NIAID

GRANT: P30 AI42845-08

ACRONYM: AI

MEDLINETA: Biochimie

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