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1H NMR characterization of two crambin species
Institution:1. Philips Medical Systems, PO Box 218, 5600 MD Eindhoven, The Netherlands;2. Department of Chemistry, Ohio State University, 140 West 18th Avenue, Columbus, OH 43210, USA;3. Istituto di Chimica delle Macromolecole del CNR, Via E. Bassini 15, I-20133, Milano, Italy;4. Department of Chemistry, Carnegie Mellon University, 4400 Fifth Avenue, Pittsburgh, PA 15213, USA
Abstract:Crambin displays amino acid heterogeneity at positions 22 (Pro or Ser) and 25 (Leu or Ile). Using reversed phase HPLC the crambin mixture can be resolved into two protein fractions. It is shown by amino acid analysis and NMR spectroscopy that these fractions represent single proteins (Ser-22/Ile-25 and Pro-22/ Leu-25 species). A first characterization of the 1H-NMR spectra of these species is presented.
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