Nuclear magnetic resonance studies of the snake toxin echistatin

Open Access
Publisher Website
Google Scholar
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.

This publication has 25 references indexed in Scilit: