@article { ISI:000266794200005,
	title = {The Chitopentaose Complex of a Mutant Hen Egg-White Lysozyme Displays No Distortion of the-1 Sugar Away from a C-4(1) Chair Conformation},
	journal = {AUSTRALIAN JOURNAL OF CHEMISTRY},
	volume = {62},
	number = {6},
	year = {2009},
	note = {Symposium on Glycoscience, Chemistry and Chemical Biology, Oslo, NORWAY, 2007},
	pages = {528-532},
	abstract = {Glycosidase inhibitors frequently reflect either the charge or the {\textquoteleft}flattened{\textquoteright} shape of the oxocarbenium-ion like transition state. Much of the impetus for such inhibitory strategies derives from historical studies on ligand binding to hen egg white lysozyme (HEWL); not least those suggesting that product complexes of the enzyme showed distortion of the pyranosides in the -1 subsite. Ironically, while distortion is undoubtedly a defining feature of glycosidases, product complexes themselves are rarely distorted. Here we show that the chitopentaose product complex of a mutant E35Q HEWL, solved at 1.8 angstrom resolution, is bound with all sugars in C-4(1) conformation.},
	issn = {0004-9425},
	doi = {10.1071/CH09038},
	author = {Davies, Gideon J. and Withers, Stephen G. and Vocadlo, David J.}
}
