DEER distance measurements on proteins

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JESCHKE, Gunnar, 2012. DEER distance measurements on proteins. In: Annual Review of Physical Chemistry. 63(1), pp. 419-446. ISSN 0066-426X. eISSN 1545-1593. Available under: doi: 10.1146/annurev-physchem-032511-143716

@article{Jeschke2012dista-22650, title={DEER distance measurements on proteins}, year={2012}, doi={10.1146/annurev-physchem-032511-143716}, number={1}, volume={63}, issn={0066-426X}, journal={Annual Review of Physical Chemistry}, pages={419--446}, author={Jeschke, Gunnar} }

<rdf:RDF xmlns:dcterms="" xmlns:dc="" xmlns:rdf="" xmlns:bibo="" xmlns:dspace="" xmlns:foaf="" xmlns:void="" xmlns:xsd="" > <rdf:Description rdf:about=""> <dcterms:rights rdf:resource=""/> <dc:creator>Jeschke, Gunnar</dc:creator> <dcterms:isPartOf rdf:resource=""/> <dc:date rdf:datatype="">2013-04-30T14:43:47Z</dc:date> <dcterms:available rdf:datatype="">2013-04-30T14:43:47Z</dcterms:available> <dc:rights>terms-of-use</dc:rights> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dcterms:issued>2012</dcterms:issued> <dcterms:bibliographicCitation>Annual Review of Physical Chemistry ; 63 (2012). - S. 419-446</dcterms:bibliographicCitation> <dc:language>eng</dc:language> <dcterms:title>DEER distance measurements on proteins</dcterms:title> <dc:contributor>Jeschke, Gunnar</dc:contributor> <dspace:isPartOfCollection rdf:resource=""/> <bibo:uri rdf:resource=""/> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dcterms:abstract xml:lang="eng">Distance distributions between paramagnetic centers in the range of 1.8 to 6 nm in membrane proteins and up to 10 nm in deuterated soluble proteins can be measured by the DEER technique. The number of paramagnetic centers and their relative orientation can be characterized. DEER does not require crystallization and is not limited with respect to the size of the protein or protein complex. Diamagnetic proteins are accessible by site-directed spin labeling. To characterize structure or structural changes, experimental protocols were optimized and techniques for artifact suppression were introduced. Data analysis programs were developed, and it was realized that interpretation of the distance distributions must take into account the conformational distribution of spin labels. First methods have appeared for deriving structural models from a small number of distance constraints. The present scope and limitations of the technique are illustrated.</dcterms:abstract> </rdf:Description> </rdf:RDF>

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