edoc

Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings

Jensen, M. R. and Markwick, P. R. L. and Meier, S. and Griesinger, C. and Zweckstetter, M. and Grzesiek, S. and Bernado, P. and Blackledge, M.. (2009) Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings. Structure, 17 (9). pp. 1169-1185.

Full text not available from this repository.

Official URL: http://edoc.unibas.ch/dok/A5258752

Downloads: Statistics Overview

Abstract

Intrinsically disordered proteins (IDPs) inhabit a conformational landscape that is too complex to be described by classical structural biology, posing an entirely new set of questions concerning the molecular understanding of functional biology. The characterization of the conformational properties of IDPs, and the elucidation of the role they play in molecular function, is therefore one of the major challenges remaining for modern structural biology. NMR is the technique of choice for studying this class of proteins, providing information about structure, flexibility, and interactions at atomic resolution even in completely disordered states. In particular, residual dipolar couplings (RDCs) have been shown to be uniquely sensitive and powerful tools for characterizing local and long-range structural behavior in disordered proteins. In this review we describe recent applications of RDCs to quantitatively describe the level of local structure and transient long-range order in IDPs involved in viral replication, neurodegenerative disease, and cancer.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Grzesiek)
UniBasel Contributors:Grzesiek, Stephan
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Cell Press
ISSN:0969-2126
e-ISSN:1878-4186
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:23 Nov 2017 15:17
Deposited On:22 Mar 2012 13:20

Repository Staff Only: item control page