| DOI | Resolve DOI: https://doi.org/10.1016/0167-4838(92)90353-F |
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| Author | Search for: Ismail, Ashraf, A.1; Search for: Mantsch, Henry H.1; Search for: Wong, Patrick T. T.1 |
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| Affiliation | - National Research Council Canada. NRC Steacie Institute for Molecular Sciences
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| Format | Text, Article |
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| Subject | high pressure; temperature; protein; aggregation; secondary structure; infrared spectroscopy; denaturation |
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| Abstract | 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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| Publication date | 1992-05-22 |
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| Publisher | Elsevier |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| NRC number | NRC-IBD-40 |
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| NPARC number | 9148508 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | 888a703f-dbe0-42dd-b731-62d22baa4690 |
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| Record created | 2009-06-25 |
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| Record modified | 2020-04-24 |
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