1H NMR studies at 360 Mhz of the methyl groups in native and chemically modified basic pancreatic trypsin inhibitor (BPTI) |
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| Authors: | Antonio De Marco Harald Tschesche Gerhard Wagner Kurt Wüthrich |
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| Affiliation: | (1) Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule, CH-8093 Zürich-Hönggerberg, Switzerland;(2) Organisch-chemisches Laboratorium, Lehrstuhl für Organische Chemie und Biochemie, Technische UniversitÄt München, D-8000 München, Federal Republic of Germany;(3) Present address: Istituto di Chimica delle Macromolecole del CNR, Via Alfonso Corti, 12, I-20133 Milano, Italy |
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| Abstract: | In the 1H NMR spectra obtained at 360 MHz after digital resolution enhancement, the multiplet resonances of the methyl groups in the basic pancreatic trypsin inhibitor (BPTI) were resolved. With suitable double irradiation techniques the individual methyl resonances were assigned to the different types of aliphatic amino acid residues. Furthermore, from pH titration and comparison of the native protein with chemically modified BPTI, the resonance lines of Ala 16 in the active site and Ala 58 at the C-terminus were identified. Potential applications of the resolved methyl resonances as natural NMR probes for studies of the molecular conformations are discussed. |
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| Keywords: | NMR Proteinase inhibitor Protein modification Protein structure Basic pancreatic trypsin inhibitor |
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