CoNSEnsX+ Webserver for the Analysis of Protein Structural Ensembles Reflecting Experimentally Determined Internal Dynamics
Author:
Affiliation:
1. Faculty of Information Technology and Bionics, Pázmány Péter Catholic University, 1083 Budapest, Práter u. 50/A, Hungary
Funder
Nemzeti Kutat?si, Fejleszt?si ?s Innov?ci?s Hivatal
Publisher
American Chemical Society (ACS)
Subject
Library and Information Sciences,Computer Science Applications,General Chemical Engineering,General Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jcim.7b00066
Reference47 articles.
1. Structural Characterization of Intrinsically Disordered Proteins by NMR Spectroscopy
2. Describing intrinsically disordered proteins at atomic resolution by NMR
3. Structure and Dynamics of the Integrin LFA-1 I-Domain in the Inactive State Underlie its Inside-Out/Outside-In Signaling and Allosteric Mechanisms
4. Ensemble-Based Interpretations of NMR Structural Data to Describe Protein Internal Dynamics
5. pE-DB: a database of structural ensembles of intrinsically disordered and of unfolded proteins
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2. DIPEND: An Open-Source Pipeline to Generate Ensembles of Disordered Segments Using Neighbor-Dependent Backbone Preferences;Biomolecules;2021-10-12
3. Ensemble-Based Analysis of the Dynamic Allostery in the PSD-95 PDZ3 Domain in Relation to the General Variability of PDZ Structures;International Journal of Molecular Sciences;2020-11-06
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5. Evaluation and Selection of Dynamic Protein Structural Ensembles with CoNSEnsX+;Methods in Molecular Biology;2020
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