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• W2135131794 abstract "Controlled proteolysis of epidermal growth factor from the mouse leads to fragments of mouse epidermal growth factor containing residues 1-48 and 1-45. The COOH-terminal pentapeptide appears to play a crucial role in determining the hydrophobic interactions between the hormone and the stationary phase during gel chromatography on TSK-125 gel. Proton NMR studies indicate that the overall structure of mouse epidermal growth factor is retained in the protein devoid of the COOH-terminal pentapeptide, while subsequent cleavage of the peptide bond between Arg-45 and Asp-46 starts to perturb the proton resonances most characteristic of the tertiary structure of the hormone, especially those from the aromatic ring protons of Tyr-37. Consequently, photochemically induced dynamic nuclear polarization experiments show an increased exposure of Tyr-37 in the fragment of mouse epidermal growth factor containing residues 1-48. Nuclear Overhauser data suggest that structural changes do occur on fragmentation but seem to be localized in the tiered-beta-sheet domain which contains Tyr-37." @default.
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• W2135131794 date "1986-10-01" @default.
• W2135131794 modified "2023-10-16" @default.
• W2135131794 title "Proton NMR and photochemically induced dynamic nuclear polarization studies of peptide fragments obtained by controlled proteolysis of mouse epidermal growth factor." @default.
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• W2135131794 doi "https://doi.org/10.1016/s0021-9258(18)67048-6" @default.
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