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• W1833154410 abstract "The 1H-NMR spectrum of the snake toxin echistatin has been assigned using homonuclear two-dimensional methods. Consideration of the NOE patterns, coupling constants and putative hydrogen bonds enabled two regular features of secondary structure to be deduced: a β-sheet/turn between residues 8 and 13 and a small antiparallel β-sheet and bulge linking residues 16–20 with residues 30–33. The recognition region of the protein containing the residues RGD lies in a loop joining the two strands of the β-sheet. The β-bulge and the loop containing the RGD sequence undergo pH-dependent conformational interconversion, modulated by the side chain of Asp29." @default.
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• W1833154410 date "1991-12-01" @default.
• W1833154410 modified "2023-10-15" @default.
• W1833154410 title "Nuclear magnetic resonance studies of the snake toxin echistatin. 1H resonance assignments and secondary structure" @default.
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• W1833154410 doi "https://doi.org/10.1111/j.1432-1033.1991.tb16379.x" @default.
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