| DOI | Resolve DOI: https://doi.org/10.1111/j.1432-1033.1992.tb16942.x |
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| Author | Search for: Hollósi, Miklos; Search for: Ismail, Ashraf A.1; Search for: Mantsch, Henry H.1; Search for: Penke, Botond; Search for: Varadi, Istvan G.; Search for: Toth, Gabor K.; Search for: Laczkó, Ilona; Search for: Kurucz, Istvan; Search for: Nagy, Zoltan; Search for: Fasman, Gerald D.; Search for: Rajnavölgyi, Eva |
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| Affiliation | - National Research Council of Canada. NRC Steacie Institute for Molecular Sciences
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| Format | Text, Article |
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| Abstract | The functionally active part of influenza virus hemagglutinin was investigated through the synthesis of a series of peptides representing different parts of the intersubunit region. Secondary structure prediction, circular dichroism and Fourier transform infrared spectroscopic studies were undertaken to investigate the secondary structure of these peptides. The peptide fragments were found to adopt multiple conformations, depending on their concentration in solution, the presence of the non-ionic detergent octyl-β-d-glucoside and the polarity of the solvent. The results of biological studies with these peptide fragments are discussed in relation to their conformation, as inferred from the spectroscopic analysis. |
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| Publication date | 1992-06 |
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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-36 |
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| NPARC number | 9147803 |
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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 | 03e06b69-e29f-49e5-a736-4da2463b4df1 |
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| Record created | 2009-06-25 |
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| Record modified | 2020-04-24 |
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