@article {4406,
	title = {Assigning the NMR spectra of aromatic amino acids in proteins: analysis of two Ets pointed domains},
	journal = {Biochemistry and Cell Biology-Biochimie Et Biologie Cellulaire},
	volume = {76},
	number = {2-3},
	year = {1998},
	note = {ISI Document Delivery No.: 157QRTimes Cited: 11Cited Reference Count: 34},
	pages = {379-390},
	type = {Article},
	abstract = {The measurement of interproton nuclear Overhauser enhancements (NOEs) and dihedral angle restraints of aromatic amino acids is a critical step towards determining the structure of a protein. The complete assignment of the resonances from aromatic rings and the subsequent resolution and identification of their associated NOEs, however, can be a difficult task. Shown here is a strategy for assigning the H-1,C-13, and N-15 signals from the aromatic side chains of histidine, tryptophan, tyrosine, and phenylalanine using a suite of homo- and hetero-nuclear scalar and NOE correlation experiments, as well as selective deuterium isotope labelling. In addition, a comparison of NOE information obtained from homonuclear NOE spectroscopy (NOESY) and C-13-edited NOESY - heteronuclear single quantum correlation experiments indicates that high-resolution homonuclear two-dimensional NOESY spectra of selectively deuterated proteins are invaluable for obtaining distance restraints to the aromatic residues.},
	keywords = {ACTIVE-SITE, ANGLE, aromatic residue, BACKBONE H-1, C-13-LABELED PROTEINS, CHEMICAL-SHIFTS, dihedral, DNA-BINDING, HETERONUCLEAR NMR, HISTIDINE-RESIDUES, MAGNETIC-RESONANCE SPECTROSCOPY, NMR assignment, NOE, pH titration, PHENYLALANINE RESIDUES, TRANSCRIPTION FACTOR},
	isbn = {0829-8211},
	url = {<Go to ISI>://000078073600026},
	author = {Slupsky, C. M. and Gentile, L. N. and McIntosh, L. P.}
}
@article {3708,
	title = {Interaction of soluble cellooligosaccharides with the N-terminal cellulose-binding domain of Cellulomonas fimi CenC .2. NMR and ultraviolet absorption spectroscopy},
	journal = {Biochemistry},
	volume = {35},
	number = {44},
	year = {1996},
	note = {ISI Document Delivery No.: VR098Times Cited: 68Cited Reference Count: 46},
	month = {Nov},
	pages = {13895-13906},
	type = {Article},
	abstract = {The N-terminal cellulose-binding domain (CBDN1) from Cellulomonas fimi beta-1,4-glucanase CenC binds amorphous but not crystalline cellulose. To investigate the structural and thermodynamic bases of cellulose binding, NMR and difference ultraviolet absorbance spectroscopy were used in parallel with calorimetry (Tomme, P., Creagh, A. L., Kilburn, D. G., \& Haynes, C. A., (1996) Biochemistry 35, 13885-13894] to characterize the interaction of soluble cellooligosaccharides with CBDN1 Association constants, determined from the dependence of the amide H-1 and N-15 chemical shifts of CBDN1 upon added sugar, increase from 180 +/- 60 M(-1) for cellotriose to 4 200 +/- 720 M(-1) for cellotetraose, 34 000 +/- 7 600 M(-1) for cellopentaose, and an estimate of 50 000 M(-1) for cellohexaose. This implies that the CBDN1 cellulose-binding site spans approximately five glucosyl units, On the basis of the observed patterns of amide chemical shift changes, the cellooligosaccharides bind along a five-stranded beta-sheet that forms a concave face of the jelly-roll beta-sandwich structure of CBDN1. This beta-sheet contains a strip of hydrophobic side chains flanked on both sides by polar residues, NMR and difference ultraviolet absorbance measurements also demonstrate that tyrosine, but not tryptophan, side chains may be involved in oligosaccharide binding. These results lead to a model in which CBDN1 interacts with soluble cellooligosaccharides and, by inference, with single polysaccharide chains in regions of amorphous cellulose, primarily through hydrogen bonding to the equatorial hydroxyl groups of the pyranose rings. Van der against the apolar side chains may augment binding. CBDN1 stands in marked contrast to previously characterized CBDs that absorb to crystalline cellulose via a flat binding surface dominated by exposed aromatic rings.},
	keywords = {BACKBONE H-1, CHEMICAL-SHIFTS, ESCHERICHIA-COLI, EXPRESSION, HIGH-LEVEL, NUCLEAR-MAGNETIC-RESONANCE, PROTEIN, REESEI CELLOBIOHYDROLASE-I, SEQUENCE, TRICHODERMA-REESEI, TRYPTOPHAN RESIDUES},
	isbn = {0006-2960},
	url = {<Go to ISI>://A1996VR09800005},
	author = {Johnson, P. E. and Tomme, P. and Joshi, M. D. and McIntosh, L. P.}
}
