The goal of pE-DB (http://pedb.vib.be) is to serve as an openly accessible database for the deposition of structural ensembles of intrinsically disordered proteins (IDPs) and of denatured proteins based on nuclear magnetic resonance spectroscopy, small-angle X-ray scattering and other data measured in solution. Owing to the inherent flexibility of IDPs, solution techniques are particularly appropriate for characterizing their biophysical properties, and structural ensembles in agreement with these data provide a convenient tool for describing the underlying conformational sampling. Database entries consist of (i) primary experimental data with descriptions of the acquisition methods and algorithms used for the ensemble calculations, and (ii) the structural ensembles consistent with these data, provided as a set of models in a Protein Data Bank format. PE-DB is open for submissions from the community, and is intended as a forum for disseminating the structural ensembles and the methodologies used to generate them. While the need to represent the IDP structures is clear, methods for determining and evaluating the structural ensembles are still evolving. The availability of the pE-DB database is expected to promote the development of new modeling methods and leads to a better understanding of how function arises from disordered states.

pE-DB: a database of structural ensembles of intrinsically disordered and of unfolded proteins / M. Varadi;S. Kosol;P. Lebrun;E. Valentini;M. Blackledge;A. K. Dunker;I. C. Felli;J. D. Forman-Kay;R. W. Kriwacki;R. Pierattelli;J. Sussman;D. I. Svergun;V. N. Uversky;M. Vendruscolo;D. Wishart;P. E. Wright;P. Tompa. - In: NUCLEIC ACIDS RESEARCH. - ISSN 0305-1048. - STAMPA. - 42:(2014), pp. D326-D335. [10.1093/nar/gkt960]

pE-DB: a database of structural ensembles of intrinsically disordered and of unfolded proteins

FELLI, ISABELLA CATERINA;PIERATTELLI, ROBERTA;
2014

Abstract

The goal of pE-DB (http://pedb.vib.be) is to serve as an openly accessible database for the deposition of structural ensembles of intrinsically disordered proteins (IDPs) and of denatured proteins based on nuclear magnetic resonance spectroscopy, small-angle X-ray scattering and other data measured in solution. Owing to the inherent flexibility of IDPs, solution techniques are particularly appropriate for characterizing their biophysical properties, and structural ensembles in agreement with these data provide a convenient tool for describing the underlying conformational sampling. Database entries consist of (i) primary experimental data with descriptions of the acquisition methods and algorithms used for the ensemble calculations, and (ii) the structural ensembles consistent with these data, provided as a set of models in a Protein Data Bank format. PE-DB is open for submissions from the community, and is intended as a forum for disseminating the structural ensembles and the methodologies used to generate them. While the need to represent the IDP structures is clear, methods for determining and evaluating the structural ensembles are still evolving. The availability of the pE-DB database is expected to promote the development of new modeling methods and leads to a better understanding of how function arises from disordered states.
2014
42
D326
D335
M. Varadi;S. Kosol;P. Lebrun;E. Valentini;M. Blackledge;A. K. Dunker;I. C. Felli;J. D. Forman-Kay;R. W. Kriwacki;R. Pierattelli;J. Sussman;D. I. Svergun;V. N. Uversky;M. Vendruscolo;D. Wishart;P. E. Wright;P. Tompa
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/836169
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