COMPREHENSIVE NOE CHARACTERIZATION OF A PARTIALLY FOLDED LARGE FRAGMENT OF STAPHYLOCOCCAL NUCLEASE DELTA-131-DELTA, USING NMR METHODS WITH IMPROVED RESOLUTION
Ow. Zhang et al., COMPREHENSIVE NOE CHARACTERIZATION OF A PARTIALLY FOLDED LARGE FRAGMENT OF STAPHYLOCOCCAL NUCLEASE DELTA-131-DELTA, USING NMR METHODS WITH IMPROVED RESOLUTION, Journal of Molecular Biology, 272(1), 1997, pp. 9-20
Comprehensive NOE results from detailed structural characterization of
a 131 residue partially folded fragment of staphylococcal nuclease (D
elta 131 Delta) made possible by NMR methods with improved resolution
are presented. The resulting NOE patterns reflect sampling of both alp
ha and beta regions of phi, phi conformational space, yet demonstrate
significant preferences for both native-like and non-native-like turn
and potentially helical conformations. Together with data from studies
of the unfolded state of the drkN SH3 domain, NOE patterns observed f
or partially folded or unfolded proteins are summarized. It is surpris
ing that few long-range NOEs were observed in Delta 131 Delta. The two
longest-range NOEs are both native-like; one of these, an (i,i + 5) N
OE, provides evidence for a Schellman capping motif for helix terminat
ion. Many aliphatic-aliphatic and aliphatic-amide NOEs, which are not
normally observed in folded proteins, were detected. We have ruled out
significant contributions from spin-diffusion for a number of these N
OEs and suggest that one source may be sampling of non-prolyl cis pept
ide bond configurations in the disordered state of Delta 131 Delta. (C
) 1997 Academic Press Limited.