dc.creatorMonasterio Opazo, Octavio
dc.creatorNowak, Thomas
dc.date.accessioned2018-12-20T14:41:19Z
dc.date.available2018-12-20T14:41:19Z
dc.date.created2018-12-20T14:41:19Z
dc.date.issued1996
dc.identifierBiological Research, Volumen 29, Issue 1, 2018, Pages 141-163
dc.identifier07169760
dc.identifierhttp://repositorio.uchile.cl/handle/2250/157047
dc.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.
dc.languageen
dc.rightshttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
dc.sourceBiological Research
dc.subjectEnzyme-ligand interactions
dc.subjectNuclear magnetic resonance (NMR)
dc.subjectSolvent relaxation
dc.titleApplications of nuclear magnetic resonance to determine the structure and interactions of ligands, peptides and enzymes
dc.typeArtículos de revistas


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