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Author dc.contributor.author Monasterio Opazo, Octavio
Author dc.contributor.author Nowak, Thomas
Admission date dc.date.accessioned 2018-12-20T14:41:19Z
Available date dc.date.available 2018-12-20T14:41:19Z
Publication date dc.date.issued 1996
Cita de ítem dc.identifier.citation Biological Research, Volumen 29, Issue 1, 2018, Pages 141-163
Identifier dc.identifier.issn 07169760
Identifier dc.identifier.uri https://repositorio.uchile.cl/handle/2250/157047
Abstract dc.description.abstract Nuclear 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.
Lenguage dc.language.iso en
Type of license dc.rights Attribution-NonCommercial-NoDerivs 3.0 Chile
Link to License dc.rights.uri http://creativecommons.org/licenses/by-nc-nd/3.0/cl/
Source dc.source Biological Research
Keywords dc.subject Enzyme-ligand interactions
Keywords dc.subject Nuclear magnetic resonance (NMR)
Keywords dc.subject Solvent relaxation
Título dc.title Applications of nuclear magnetic resonance to determine the structure and interactions of ligands, peptides and enzymes
Document type dc.type Artículo de revista
Cataloguer uchile.catalogador SCOPUS
Indexation uchile.index Artículo de publicación SCOPUS
uchile.cosecha uchile.cosecha SI
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Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivs 3.0 Chile