Facets (new session)
Description
Metadata
Settings
owl:sameAs
Inference Rule:
b3s
b3sifp
dbprdf-label
facets
http://dbpedia.org/resource/inference/rules/dbpedia#
http://dbpedia.org/resource/inference/rules/opencyc#
http://dbpedia.org/resource/inference/rules/umbel#
http://dbpedia.org/resource/inference/rules/yago#
http://dbpedia.org/schema/property_rules#
http://www.ontologyportal.org/inference/rules/SUMO#
http://www.ontologyportal.org/inference/rules/WordNet#
http://www.w3.org/2002/07/owl#
ldp
oplweb
skos-trans
virtrdf-label
None
About:
The impact of protein characterization in structural proteomics
Goto
Sponge
NotDistinct
Permalink
An Entity of Type :
schema:ScholarlyArticle
, within Data Space :
wasabi.inria.fr
associated with source
document(s)
Type:
Academic Article
research paper
schema:ScholarlyArticle
New Facet based on Instances of this Class
Attributes
Values
type
Academic Article
research paper
schema:ScholarlyArticle
isDefinedBy
Covid-on-the-Web dataset
has title
The impact of protein characterization in structural proteomics
Creator
Brown, J
Gilbert, R
Coutard, B
Nordlund, P
Owens, R
Svergun, D
Egloff, M.-P
Enguita, F
Fogg, M
Geerlof, Arie
Groves, M
Haouz, A
Nettleship, J
Ruff, M
Sainsbury, S
Wilmanns, Matthias
Source
Medline; PMC
abstract
Protein characterization plays a role in two key aspects of structural proteomics. The first is the quality assessment of the produced protein preparations. Obtaining well diffracting crystals is one of the major bottlenecks in the structure‐determination pipeline. Often, this is caused by the poor quality of the protein preparation used for crystallization trials. Hence, it is essential to perform an extensive quality assessment of the protein preparations prior to crystallization and to use the results in the evaluation of the process. Here, a protein‐production and crystallization strategy is proposed with threshold values for protein purity (95%) and monodispersity (85%) below which a further optimization of the protein‐production process is strongly recommended. The second aspect is the determination of protein characteristics such as domains, oligomeric state, post‐translational modifications and protein–protein and protein–ligand interactions. In this paper, applications and new developments of protein‐characterization methods using MS, fluorescence spectroscopy, static light scattering, analytical ultracentrifugation and small‐angle X‐ray scattering within the EC Structural Proteomics in Europe contract are described. Examples of the application of the various methods are given.
has issue date
2006-10-04
(
xsd:dateTime
)
bibo:doi
10.1107/s0907444906030307
bibo:pmid
17001090
has license
no-cc
sha1sum (hex)
220f9a2fbceef0d3c30b3f7a346946c3a125e183
schema:url
https://doi.org/10.1107/s0907444906030307
resource representing a document's title
The impact of protein characterization in structural proteomics
has PubMed Central identifier
PMC7161605
has PubMed identifier
17001090
schema:publication
Acta Crystallogr D Biol Crystallogr
resource representing a document's body
covid:220f9a2fbceef0d3c30b3f7a346946c3a125e183#body_text
is
schema:about
of
named entity 'evaluation'
named entity 'pipeline'
named entity 'bottlenecks'
named entity 'interactions'
named entity 'caused'
named entity 'impact'
named entity 'Europe'
named entity 'preparation'
named entity 'process'
named entity 'Here'
named entity 'determination'
named entity 'protein'
named entity 'protein-protein'
named entity 'crystallization'
named entity 'crystallization'
named entity 'protein'
named entity 'static light scattering'
named entity 'protein'
named entity 'protein'
named entity 'monodispersity'
named entity 'protein'
named entity 'molecular function'
named entity 'dimer'
named entity 'X-ray'
named entity 'peptide'
named entity 'protein'
named entity 'D'Arcy'
named entity 'DLS'
named entity 'ligands'
named entity 'Sedimentation coefficient'
named entity 'aggregation state'
named entity 'NADPH'
named entity 'scattering'
named entity 'correlation'
named entity 'biophysical properties'
named entity 'protein'
named entity 'ligands'
named entity 'kDa'
named entity 'crystallization'
named entity 'protein'
named entity 'protein'
named entity 'quality assessment'
named entity 'purification process'
named entity 'virial coefficient'
named entity 'single-domain'
named entity 'phosphorylated protein'
named entity 'signalling molecule'
named entity 'pro-apoptotic'
named entity 'dengue virus'
named entity 'crystallization'
named entity 'protein'
named entity 'structure determination'
named entity 'protein'
named entity 'protein'
named entity 'sedimentation coefficient'
named entity 'correlation'
named entity 'asparagine'
named entity 'crystallization'
named entity 'optical density'
named entity 'N-terminal'
named entity 'glycosylation'
named entity 'chromophoric'
named entity 'lysine'
named entity 'crystallization'
named entity 'AUC'
named entity 'scattering'
◂◂ First
◂ Prev
Next ▸
Last ▸▸
Page 1 of 11
Go
Faceted Search & Find service v1.13.91 as of Mar 24 2020
Alternative Linked Data Documents:
Sponger
|
ODE
Content Formats:
RDF
ODATA
Microdata
About
OpenLink Virtuoso
version 07.20.3229 as of Jul 10 2020, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (94 GB total memory)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software