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Authordc.contributor.authorMonasterio Opazo, Octavio 
Authordc.contributor.authorNowak, Thomas 
Admission datedc.date.accessioned2018-12-20T14:41:19Z
Available datedc.date.available2018-12-20T14:41:19Z
Publication datedc.date.issued1996
Cita de ítemdc.identifier.citationBiological Research, Volumen 29, Issue 1, 2018, Pages 141-163
Identifierdc.identifier.issn07169760
Identifierdc.identifier.urihttps://repositorio.uchile.cl/handle/2250/157047
Abstractdc.description.abstractNuclear magnetic resonance (NMR) spectroscopy is emerging as a powerful tool for the study of enzyme structure and function. This article discusses the general principles of NMR and the potential information this technique can provide in the study of enzymes along with its limitations.
Lenguagedc.language.isoen
Type of licensedc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
Link to Licensedc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/
Sourcedc.sourceBiological Research
Keywordsdc.subjectEnzyme-ligand interactions
Keywordsdc.subjectNuclear magnetic resonance (NMR)
Keywordsdc.subjectSolvent relaxation
Títulodc.titleApplications of nuclear magnetic resonance to determine the structure and interactions of ligands, peptides and enzymes
Document typedc.typeArtículo de revista
Catalogueruchile.catalogadorSCOPUS
Indexationuchile.indexArtículo de publicación SCOPUS
uchile.cosechauchile.cosechaSI


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Attribution-NonCommercial-NoDerivs 3.0 Chile
Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivs 3.0 Chile