Literature DB >> 20399178

The meandering of disordered proteins in conformational space.

Robert Konrat1.   

Abstract

In this issue, Mittag et al. (2010) provided interesting insights concerning the molecular details of how the meandering of disordered proteins in conformational space can lead to collective binding modes and ultrasensitive probing of cellular kinase activities. Copyright 2010 Elsevier Ltd. All rights reserved.

Entities:  

Year:  2010        PMID： 20399178     DOI： 10.1016/j.str.2010.03.003

Source DB:  PubMed          Journal:  Structure        ISSN： 0969-2126            Impact factor:   5.006


  5 in total

1.  IDPs: Less Disordered and More Ordered than Expected.

Authors:  Robert Konrat
Journal:  Biophys J       Date:  2015-10-06       Impact factor: 4.033

Review 2.  How random are intrinsically disordered proteins? A small angle scattering perspective.

Authors:  Veronique Receveur-Brechot; Dominique Durand
Journal:  Curr Protein Pept Sci       Date:  2012-02       Impact factor: 3.272

3.  Probing Local Backbone Geometries in Intrinsically Disordered Proteins by Cross-Correlated NMR Relaxation.

Authors:  Jan Stanek; Saurabh Saxena; Leonhard Geist; Robert Konrat; Wiktor Koźmiński
Journal:  Angew Chem Weinheim Bergstr Ger       Date:  2013-03-20

4.  Probing local backbone geometries in intrinsically disordered proteins by cross-correlated NMR relaxation.

Authors:  Jan Stanek; Saurabh Saxena; Leonhard Geist; Robert Konrat; Wiktor Koźmiński
Journal:  Angew Chem Int Ed Engl       Date:  2013-03-20       Impact factor: 15.336

5.  Cooperative unfolding of compact conformations of the intrinsically disordered protein osteopontin.

Authors:  Dennis Kurzbach; Gerald Platzer; Thomas C Schwarz; Morkos A Henen; Robert Konrat; Dariush Hinderberger
Journal:  Biochemistry       Date:  2013-07-24       Impact factor: 3.162
  5 in total

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