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- W98982477 abstract "ABSTRACT Several solvent exposed main amide protons in basic pancreatic trypsin inhibitor exchange isotope with water at low rates of 102−104 times less than low molecular weight model compounds. Proton NMR signals of Gly-12, Ile-19, Ala25, Cys-30, Thr-32, and Val-34 NH are resolved in the 1 dimensional NMR spectrum by specific isotope labeling. Their exchange is found to be independent of the protein concentration in the range 0.2-4 mM, indicating that slow exchange is not a consequence of protein dimerization and burial at a protein-protein interface." @default.
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- W98982477 date "1987-01-01" @default.
- W98982477 modified "2023-09-26" @default.
- W98982477 title "PROPERTIES OF THE PROTEIN SOLVENT INTERFACE, STUDIED BY DEUTERIUM EXCHANGE IN BASIC PANCREATIC TRYPSIN INHIBITOR" @default.
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- W98982477 doi "https://doi.org/10.1016/b978-0-08-035588-7.50100-x" @default.
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