Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins - Science Advances
Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins - Science Advances
Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins Science AdvancesIn every established species, protein-protein interactions have evolved such that they are fit for purpose. However, the molecular details of the evolution of new ...
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04-25-2019 05:39 PM
Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins - Science Advances
Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins - Science Advances
Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins Science AdvancesIn every established species, protein-protein interactions have evolved such that they are fit for purpose. However, the molecular details of the evolution of new ...
Read here
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01-07-2019 05:49 AM
[NMR paper] Revealing Conformational Variants of Solution-Phase Intrinsically Disordered Tau Protein at the Single-Molecule Level
Revealing Conformational Variants of Solution-Phase Intrinsically Disordered Tau Protein at the Single-Molecule Level
Intrinsically disordered proteins, such as tau protein, adopt a variety of conformations in solution, complicating solution-phase structural studies. We employ an anti-Brownian electrokinetic (ABEL) trap to prolong measurements of single tau proteins in solution. Once trapped, we record the fluorescence anisotropy to investigate the diversity of conformations sampled by the single molecules. A distribution of anisotropy values obtained from trapped tau protein is...
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10-24-2017 05:09 PM
[NMR paper] Toward optimal-resolution NMR of intrinsically disordered proteins.
Toward optimal-resolution NMR of intrinsically disordered proteins.
Related Articles Toward optimal-resolution NMR of intrinsically disordered proteins.
J Magn Reson. 2014 Apr;241:41-52
Authors: Nová?ek J, Zídek L, Sklená? V
Abstract
Proteins, which, in their native conditions, sample a multitude of distinct conformational states characterized by high spatiotemporal heterogeneity, most often termed as intrinsically disordered proteins (IDPs), have become a target of broad interest over the past 15years. With the growing evidence of their...
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03-25-2014 11:49 AM
Toward optimal-resolution NMR of intrinsically disordered proteins
Toward optimal-resolution NMR of intrinsically disordered proteins
Publication date: April 2014
Source:Journal of Magnetic Resonance, Volume 241</br>
Author(s): Ji?í Nová?ek , Lukáš Žídek , Vladimír Sklená?</br>
Proteins, which, in their native conditions, sample a multitude of distinct conformational states characterized by high spatiotemporal heterogeneity, most often termed as intrinsically disordered proteins (IDPs), have become a target of broad interest over the past 15years. With the growing evidence of their important roles in fundamental cellular...