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pE-DB: a database of structural ensembles of intrinsically disordered and of unfolded proteins
- Source :
- Nucleic Acids Research, Nucleic acids symposium series 42(D1), D326-D335 (2014). doi:10.1093/nar/gkt960, Nucleic Acids Research, Oxford University Press, 2014, 42 (Database issue), pp.D326-35, Nucleic Acids Research, 2014, 42 (Database issue), pp.D326-35
- Publication Year :
- 2014
-
Abstract
- International audience; 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.
- Subjects :
- MESH: Databases, Protein
Intrinsically dosordered proteins, IDP, NMR, modeling
Biology
010402 general chemistry
Intrinsically disordered proteins
computer.software_genre
01 natural sciences
Set (abstract data type)
II. Protein sequence and structure, motifs and domains
03 medical and health sciences
Modelling methods
MESH: Nuclear Magnetic Resonance, Biomolecular
Scattering, Small Angle
Genetics
Data bank
Conformational sampling
Databases, Protein
Nuclear Magnetic Resonance, Biomolecular
MESH: Scattering, Small Angle
030304 developmental biology
Protein Unfolding
MESH: Intrinsically Disordered Proteins
Flexibility (engineering)
0303 health sciences
Internet
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM]
Database
MESH: X-Ray Diffraction
A protein
Experimental data
0104 chemical sciences
X-ray diffraction
MESH: Internet
MESH: Protein Unfolding
ddc:540
intrinsically disordered proteins
computer
Subjects
Details
- Language :
- English
- ISSN :
- 03051048 and 13624962
- Database :
- OpenAIRE
- Journal :
- Nucleic Acids Research, Nucleic acids symposium series 42(D1), D326-D335 (2014). doi:10.1093/nar/gkt960, Nucleic Acids Research, Oxford University Press, 2014, 42 (Database issue), pp.D326-35, Nucleic Acids Research, 2014, 42 (Database issue), pp.D326-35
- Accession number :
- edsair.doi.dedup.....82947363e525f17d72c4034e488d6527
- Full Text :
- https://doi.org/10.1093/nar/gkt960