[NMR paper] NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins
NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins
Intrinsically disordered proteins are ubiquitous throughout all known proteomes, playing essential roles in all aspects of cellular and extracellular biochemistry. To understand their function, it is necessary to determine their structural and dynamic behavior and to describe the physical chemistry of their interaction trajectories. Nuclear magnetic resonance is perfectly adapted to this task, providing ensemble averaged structural and dynamic parameters that report on each...
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04-22-2022 03:01 AM
Solvent saturation transfer to proteins (SSTP) for structural and functional characterization of proteins
Solvent saturation transfer to proteins (SSTP) for structural and functional characterization of proteins
Abstract
Protein structure determination using NMR is dependent on experimentally acquired distance restraints. Often, however, an insufficient number of these restraints are available for determining a proteinā??s correct fold, much less its detailed three-dimensional structure. In consideration of this problem, we propose a simple means to acquire supplemental structural restraints from protein surface accessibilities using solvent saturation...
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11-30-2017 05:01 PM
Using Isothermal Titration Calorimetry for Biophysical Characterization of Chromatin-Binding Proteins - News-Medical.net
Using Isothermal Titration Calorimetry for Biophysical Characterization of Chromatin-Binding Proteins - News-Medical.net
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Using Isothermal Titration Calorimetry for Biophysical Characterization of Chromatin-Binding Proteins
News-Medical.net
Structural studies like nuclear magnetic resonance (NMR) and X-ray crystallography provide additional validation and characterization. This article describes the...
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11-19-2016 08:35 PM
An assignment of intrinsically disordered regions of proteins based on NMR structures
An assignment of intrinsically disordered regions of proteins based on NMR structures
January 2013
Publication year: 2013
Source:Journal of Structural Biology, Volume 181, Issue 1</br>
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Intrinsically disordered proteins (IDPs) do not adopt stable three-dimensional structures in physiological conditions, yet these proteins play crucial roles in biological phenomena. In most cases, intrinsic disorder manifests itself in segments or domains of an IDP, called intrinsically disordered regions (IDRs), but fully disordered IDPs also exist. Although IDRs can be detected as...
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02-03-2013 10:13 AM
[KPWU blog] Web Severs for prediction of disordered regions (DRs) in proteins
Web Severs for prediction of disordered regions (DRs) in proteins
This list of web severs is obtained from the published paper “Evaluation of disorder predictions in CASP9” by*Andriy Kryshtafovych. List of web servers and the methods descriptions (copy from table III of Kryshtafovych’s paper). Please read the paper for details of methods and performance. PrDOS2*(http://prdos.hgc.jp/cgi-bin/top.cgi) SVM algorithm based on sequence profiles combined with a template-based http://stats.wordpress.com/b.gif?host=kpwu.wordpress.com&blog=76132&post=513&subd=kpwu&ref=&feed=1
Go to KPWU blog to...