UNIVERSI
TÄ
TS-
BIBLIOTHEK
P
ADERBORN
Anmelden
Menü
Menü
Start
Hilfe
Blog
Weitere Dienste
Neuerwerbungslisten
Fachsystematik Bücher
Erwerbungsvorschlag
Bestellung aus dem Magazin
Fernleihe
Einstellungen
Sprache
Deutsch
Deutsch
Englisch
Farbschema
Hell
Dunkel
Automatisch
Sie befinden Sich nicht im Netzwerk der Universität Paderborn. Der Zugriff auf elektronische Ressourcen ist
gegebenenfalls
nur via VPN oder Shibboleth (DFN-AAI) möglich.
mehr Informationen...
Universitätsbibliothek
Katalog
Suche
Details
Zur Ergebnisliste
Ergebnis 47 von 130
Datensatz exportieren als...
BibTeX
HingeProt: Automated prediction of hinges in protein structures
Proteins, structure, function, and bioinformatics, 2008-03, Vol.70 (4), p.1219-1227
Emekli, Ugur
Schneidman-Duhovny, Dina
Wolfson, Haim J.
Nussinov, Ruth
Haliloglu, Turkan
2008
Volltextzugriff (PDF)
Details
Autor(en) / Beteiligte
Emekli, Ugur
Schneidman-Duhovny, Dina
Wolfson, Haim J.
Nussinov, Ruth
Haliloglu, Turkan
Titel
HingeProt: Automated prediction of hinges in protein structures
Ist Teil von
Proteins, structure, function, and bioinformatics, 2008-03, Vol.70 (4), p.1219-1227
Ort / Verlag
Hoboken: Wiley Subscription Services, Inc., A Wiley Company
Erscheinungsjahr
2008
Quelle
MEDLINE
Beschreibungen/Notizen
Proteins are highly flexible molecules. Prediction of molecular flexibility aids in the comprehension and prediction of protein function and in providing details of functional mechanisms. The ability to predict the locations, directions, and extent of molecular movements can assist in fitting atomic resolution structures to low‐resolution EM density maps and in predicting the complex structures of interacting molecules (docking). There are several types of molecular movements. In this work, we focus on the prediction of hinge movements. Given a single protein structure, the method automatically divides it into the rigid parts and the hinge regions connecting them. The method employs the Elastic Network Model, which is very efficient and was validated against a large data set of proteins. The output can be used in applications such as flexible protein–protein and protein–ligand docking, flexible docking of protein structures into cryo‐EM maps, and refinement of low‐resolution EM structures. The web server of HingeProt provides convenient visualization of the results and is available with two mirror sites at http://www.prc.boun.edu.tr/appserv/prc/HingeProt3 and http://bioinfo3d.cs.tau.ac.il/HingeProt/. Proteins 2008. © 2007 Wiley‐Liss, Inc.
Sprache
Englisch
Identifikatoren
ISSN: 0887-3585
eISSN: 1097-0134
DOI: 10.1002/prot.21613
Titel-ID: cdi_proquest_miscellaneous_70339966
Format
–
Schlagworte
Computational Biology - methods
,
Computer Simulation
,
Databases, Protein
,
docking
,
hinges
,
Internet
,
Ligands
,
Models, Molecular
,
Movement
,
NMA
,
Protein Binding
,
Protein Conformation
,
protein flexibility
,
protein function
,
Proteins - chemistry
Weiterführende Literatur
Empfehlungen zum selben Thema automatisch vorgeschlagen von
bX