dc.creator | Monasterio Opazo, Octavio | |
dc.creator | Nowak, Thomas | |
dc.date.accessioned | 2018-12-20T14:41:19Z | |
dc.date.available | 2018-12-20T14:41:19Z | |
dc.date.created | 2018-12-20T14:41:19Z | |
dc.date.issued | 1996 | |
dc.identifier | Biological Research, Volumen 29, Issue 1, 2018, Pages 141-163 | |
dc.identifier | 07169760 | |
dc.identifier | http://repositorio.uchile.cl/handle/2250/157047 | |
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. | |
dc.language | en | |
dc.rights | http://creativecommons.org/licenses/by-nc-nd/3.0/cl/ | |
dc.rights | Attribution-NonCommercial-NoDerivs 3.0 Chile | |
dc.source | Biological Research | |
dc.subject | Enzyme-ligand interactions | |
dc.subject | Nuclear magnetic resonance (NMR) | |
dc.subject | Solvent relaxation | |
dc.title | Applications of nuclear magnetic resonance to determine the structure and interactions of ligands, peptides and enzymes | |
dc.type | Artículos de revistas | |