Bitte benutzen Sie diese Kennung, um auf die Ressource zu verweisen: http://dspace.utpl.edu.ec/handle/123456789/18925
Langanzeige der Metadaten
DC ElementWertSprache
dc.contributor.authorAusili, A.es_ES
dc.date.accessioned2017-06-16T22:02:37Z-
dc.date.available2017-06-16T22:02:37Z-
dc.date.submitted23/10/2015es_ES
dc.identifier10.3233/BSI-150104es_ES
dc.identifier.isbn2212-8794es_ES
dc.identifier.other10.3233/BSI-150104es_ES
dc.identifier.urihttp://dspace.utpl.edu.ec/handle/123456789/18925-
dc.description.abstractOne of the most powerful techniques used to gain structural information of membrane proteins is the Attenuated Total Reflectance Fourier Transformed Infrared spectroscopy (ATR-FTIR). Secondary structure, conformational changes, interactions with lipids and spatial positioning of membranes, proteins and peptides are commonly analyzed by this method that allows having a simultaneous vision of the membrane and the protein that is bound. In particular, ATR-FTIR is especially advantageous to evaluate the membrane lipids order and the effective position of a protein relative to the membrane. This technique has been successfully applied to study alpha-helical peptides and proteins, and also beta-sheet, beta-barrel and beta-sandwich proteins, but potentially it could be applicable for any protein structure suitable for a geometric approximation. The present review wants to examine and summarize the different models developed to calculate the orientation of these proteins giving some practical examples, analyzing lipid alignment, protein secondary structure and orientation.es_ES
dc.languageIngléses_ES
dc.subjectATR-FTIRes_ES
dc.subjectdichroismes_ES
dc.subjectsecondary structurees_ES
dc.subjectprotein and lipid orientationes_ES
dc.titleAttenuated total reflectance infrared spectroscopy: A powerful method for the simultaneous study of structure and spatial orientation of lipids and membrane proteinses_ES
dc.typeArticlees_ES
dc.publisherBIOMEDICAL SPECTROSCOPY AND IMAGINGes_ES
Enthalten in den Sammlungen:Artículos de revistas Científicas

Dateien zu dieser Ressource:


Alle Ressourcen in diesem Repository sind urheberrechtlich geschützt.