13C NMR spectral assignment of ribonuclease S-peptide. Some new structural information about its low-temperature folding |
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| Affiliation: | 1. Institute for Applied Geophysics and Geothermal Energy (GGE), FEN Research Campus, RWTH Aachen University, 52074 Aachen, Germany;2. Institute for Power Generation and Storage Systems (PGS), FEN Research Campus, RWTH Aachen University, 52074 Aachen, Germany;1. Department of Civil Engineering, Razi University, Kermanshah, Iran;2. Department of Computer System, Faculty of Computer Science and Information Technology, University of Malaya, 50603 Kuala Lumpur, Malaysia;3. Department of Civil Engineering, Faculty of Engineering Building, University of Malaya, 50603 Kuala Lumpur, Malaysia;4. University of Nis, Faculty of Mechanical Engineering, Department for Mechatronics and Control, Aleksandra Medvedeva 14, 18000 Nis, Serbia;1. Service des urgences pédiatriques et post-urgences, hôpital des enfants groupe Pellegrin, place Amélie-Rabat-Léon, 33000 Bordeaux, France;2. Clinique médicale et service d’urgences pédiatriques, hôpital Mère-Enfant, 8, quai Moncousu, 44000 Nantes, France;3. Service de réanimation néonatale, CHU de Martinique, site de la Maison-de-la-Femme, de la Mère-et-de l’Enfant, 97200 Fort-de-France, Martinique |
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| Abstract: | 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. |
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