| DOI | Trouver le DOI : https://doi.org/10.1016/0167-4838(92)90353-F |
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| Auteur | Rechercher : Ismail, Ashraf, A.1; Rechercher : Mantsch, Henry H.1; Rechercher : Wong, Patrick T. T.1 |
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| Affiliation | - Conseil national de recherches du Canada. Institut Steacie des sciences moléculaires du CNRC
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| Format | Texte, Article |
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| Sujet | high pressure; temperature; protein; aggregation; secondary structure; infrared spectroscopy; denaturation |
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| Résumé | Changes in the secondary structure and aggregation of chymotrypsinogen were investigated by infrared difference spectroscopy in conjunction with temperature and pressure tuning IR spectroscopy; both the amide I′ band and side chain bands were studied. A prominent component of the amide I′ band in the difference spectrum obtained upon cooling a chymotrypsinogen solution, or increasing the hydrostatic pressure, was observed in the region between 1627 and 1622 cm⁻¹. Under denaturing conditions a white gel was formed, which is attributed to irreversible self-association or aggregation. This process was accompanied by the appearance of two new amide I′ bands in the infrared spectrum of the protein: a very strong band at 1618 cm⁻¹ and a weak band at 1685 cm⁻¹. These bands are assigned to peptide segments with anti-parallel aligned β-strands. |
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| Date de publication | 1992-05-22 |
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| Maison d’édition | Elsevier |
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| Dans | |
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| Langue | anglais |
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| Publications évaluées par des pairs | Oui |
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| Numéro du CNRC | NRC-IBD-40 |
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| Numéro NPARC | 9148508 |
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| Exporter la notice | Exporter en format RIS |
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| Signaler une correction | Signaler une correction (s'ouvre dans un nouvel onglet) |
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| Identificateur de l’enregistrement | 888a703f-dbe0-42dd-b731-62d22baa4690 |
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| Enregistrement créé | 2009-06-25 |
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| Enregistrement modifié | 2020-04-24 |
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