ArticleBMC structural biology2010
CoNSEnsX: an ensemble view of protein structures and NMR-derived experimental data.
Article in BMC structural biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 15 citations in OpenAlex.
- EnGens: a computational framework for generation and analysis of representative protein conformational ensembles.Briefings in bioinformatics · 2023Article
- EnGens: a computational framework for generation and analysis of representative protein conformational ensembles.bioRxiv : the preprint server for biology · 2023Article
- Allostery: Allosteric Cancer Drivers and Innovative Allosteric Drugs.Journal of molecular biology · 2022Review
- Simultaneous Assignment and Structure Determination of Proteins From Sparsely Labeled NMR Datasets.Frontiers in molecular biosciences · 2021Article
- Different modes of barrel opening suggest a complex pathway of ligand binding in human gastrotropin.PloS one · 2019Article
- Fine-tuning the extent and dynamics of binding cleft opening as a potential general regulatory mechanism in parvulin-type peptidyl prolyl isomerases.Scientific reports · 2017Article
- "Invisible" conformers of an antifungal disulfide protein revealed by constrained cold and heat unfolding, CEST-NMR experiments, and molecular dynamics calculations.Chemistry (Weinheim an der Bergstrasse, Germany) · 2015Article
- Ensemble-based interpretations of NMR structural data to describe protein internal dynamics.Molecules (Basel, Switzerland) · 2013Review
- Combining NMR ensembles and molecular dynamics simulations provides more realistic models of protein structures in solution and leads to better chemical shift prediction.Journal of biomolecular NMR · 2012Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundIn conjunction with the recognition of the functional role of internal dynamics of proteins at various timescales, there is an emerging use of dynamic structural ensembles instead of individual conformers. These ensembles are usually substantially more diverse than conventional NMR ensembles and eliminate the expectation that a single conformer should fulfill all NMR parameters originating from 10(16) - 10(17) molecules in the sample tube. Thus, the accuracy of dynamic conformational ensembles should be evaluated differently to that of single conformers.
resultsWe constructed the web application CoNSEnsX (Consistency of NMR-derived Structural Ensembles with eXperimental data) allowing fast, simple and convenient assessment of the correspondence of the ensemble as a whole with diverse independent NMR parameters available. We have chosen different ensembles of three proteins, human ubiquitin, a small protease inhibitor and a disordered subunit of cGMP phosphodiesterase 5/6 for detailed evaluation and demonstration of the capabilities of the CoNSEnsX approach.
conclusionsOur results present a new conceptual method for the evaluation of dynamic conformational ensembles resulting from NMR structure determination. The designed CoNSEnsX approach gives a complete evaluation of these ensembles and is freely available as a web service at http://consensx.chem.elte.hu.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.