A globular protein with slower amide proton exchange from an alpha helix than from antiparallel beta sheets |
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Authors: | K Wüthrich P Strop S Ebina M P Williamson |
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Institution: | Institut für Molekuarbiologie und Biophysik, Eidgenössische Technische Hochschule, CH-8093 Zürich, Switzerland |
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Abstract: | In proteinase inhibitor IIA from bull seminal plasma, which is a small globular protein with 57 amino acid residues, measurements of individual amide proton exchange rates by two-dimensional correlated 1H NMR spectroscopy (COSY) showed that the exchange was slowest for some hydrogen bonded amide groups in an alpha-helix. This contrasts with all other proteins which were so far studied in detail, where the slowest exchange rates were observed for hydrogen bonded amide protons in antiparallel beta-sheets. |
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