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Dynamics of the EGF-like Domain of Heregulin-alpha


W.J. Fairbrother, J. Liu, P.I. Pisacane, M.X. Sliwkowski, & A.G. Palmer (1998) Backbone dynamics of the EGF-like domain of heregulin-alpha. J. Mol. Biol. 279, 1149-1161.

Structural dependence of dynamical properties of the 63 residue EGF-like domain of heregulin-alpha as represented on a backbone chain trace. The 15N reduced spectral density J(0.87wH) values are coded as the width of the backbone worm (increased radii indicate larger spectral density and greater degree of conformational flexibility), Ordered and disordered regions in the NMR solution structure of the protein are depicted in cyan and violet, respectively. Residues 44-46, which are ordered in the solution structures but experience conformational exchange on microsecond-millisecond time scales are shown in red. Disulfide linkages are shown in yellow..


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Last modified 7/25/02 Kemal Eren. Send comments to agp6@columbia.edu