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Título: | 13C NMR spectral assignment of ribonuclease S-peptide. Some new structural information about its low-temperature folding |
Autor: | Santoro, Jorge CSIC; Rico, M.; Bermejo, Francisco Javier CSIC ORCID; Nieto, J. L.; Herranz, J.; Gallego, Ernesto | Fecha de publicación: | mar-1986 | Editor: | Elsevier | Citación: | Journal of Molecular Structure 141: 243- 248 (1986) | Resumen: | The 13C NMR spectrum of S-peptide (Ribonuclease 19 residue N-terminal fragment) (pH 5.4, 32°C, 12 mM in D2O has been assigned with a basis on characteristic values for 13C signals of amino acids included in short peptides, SFOR multiplicities, 1JCH reduced values and spectral pH variations. The shift vs. temperature changes have been followed in the range 0°C-50°C and the corresponding curves analyzed by using the ΔH° and ΔS° values for the helix-coil transition obtained from 1H NMR spectra. Values for chemical shifts in the coil and in the helix have been obtained in this way. Transition shifts are largest for CO and Cα resonances in the fragment 3-13, confirming that isolated S-peptide folds in a manner closely ressembling the native structure. © 1986. | Descripción: | 6 pags.; 1 fig.; 3 tabs. | Versión del editor: | http://dx.doi.org/10.1016/0022-2860(86)80329-5 | URI: | http://hdl.handle.net/10261/128085 | DOI: | 10.1016/0022-2860(86)80329-5 | Identificadores: | doi: 10.1016/0022-2860(86)80329-5 issn: 0022-2860 |
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