@article {4070,
	title = {Stereospecific assignment of the NH2 resonances from the primary amides of asparagine and glutamine side chains in isotopically labeled proteins},
	journal = {Journal of Biomolecular Nmr},
	volume = {9},
	number = {3},
	year = {1997},
	note = {ISI Document Delivery No.: XF937Times Cited: 18Cited Reference Count: 33},
	month = {Apr},
	pages = {306-312},
	type = {Article},
	abstract = {An HMQC-based pulse scheme is presented for the stereospecific assignment of asparagine and glutamine side-chain amide protons. The approach makes use of the recently developed quantitative-J correlation spectroscopy [Bar, A. et al. (1994) Methods Enzymol., 239, 79-105] to distinguish the E and Z primary amide protons and, as such, eliminates the need for assignments derived from more time-consuming and potentially ambiguous NOE methods. An application of this method to a uniformly N-15,C-13-labeled cellulose-binding domain is presented. When used in combination with a NOESY-HSQC experiment, the predominant chi(2) dihedral angles of two asparagine side chains in this protein can also be defined.},
	keywords = {ANGLE, BACKBONE AMIDE, C-13 MAGNETIZATION, dihedral, EXCITATION, H-1, HMQC spectroscopy, LARGER PROTEINS, N-15, NMR, primary amide, SATURATION, SPECTRA, SPECTROSCOPY, STEREOSPECIFIC ASSIGNMENT},
	isbn = {0925-2738},
	url = {<Go to ISI>://A1997XF93700008},
	author = {McIntosh, L. P. and Brun, E. and Kay, L. E.}
}
@article {3800,
	title = {Secondary structure and NMR assignments of Bacillus circulans xylanase},
	journal = {Protein Science},
	volume = {5},
	number = {6},
	year = {1996},
	note = {ISI Document Delivery No.: UP617Times Cited: 23Cited Reference Count: 74},
	month = {Jun},
	pages = {1118-1135},
	type = {Article},
	abstract = {Bacillus circulans xylanase (BCX) is a member of the family of low molecular weight endo-beta-(1,4)-xylanases. The main-chain H-1, C-13, and N-15 resonances of this 20.4-kDa enzyme were assigned using heteronuclear NMR experiments recorded on a combination of selectively and uniformly labeled protein samples. Using chemical shift, NOE, J coupling, and amide hydrogen exchange information, 14 beta-strands, arranged in a network of three beta-sheets, and a single cy-helix were identified in BCX. The NMR-derived secondary structure and beta-sheet topology agree closely with that observed in the crystal structure of this protein. The H-N of Ile 118 has a strongly upfield-shifted resonance at 4.03 ppm, indicative of a potential amide-aromatic hydrogen bond to the indole ring of Trp 71. This interaction, which is conserved in all low molecular weight xylanases of known structure, may play an important role in establishing the active site conformation of these enzymes. Following hen egg white and bacteriophage T4 lysozymes, B. circulans xylanase represents the third family of beta-glycanases for which extensive NMR assignments have been reported. These assignments provide the background for detailed studies of the mechanism of carbohydrate recognition and hydrolysis by this bacterial xylanase.},
	keywords = {amide-aromatic hydrogen bond, AMINO-ACID, ASSIGNMENTS, BACKBONE AMIDE, beta-glycanase, C-13-LABELED PROTEINS, C-ALPHA, chemical shift index, CHEMICAL-SHIFTS, COUPLING-CONSTANTS, LARGER PROTEINS, NMR, NUCLEAR-MAGNETIC-RESONANCE, SECONDARY STRUCTURE, SIDE-CHAIN RESONANCES, SOLVENT, SUPPRESSION, XYLANASE},
	isbn = {0961-8368},
	url = {<Go to ISI>://A1996UP61700014},
	author = {Plesniak, L. A. and Wakarchuk, W. W. and McIntosh, L. P.}
}
@article {3018,
	title = {SECONDARY STRUCTURE OF THE ETS DOMAIN PLACES MURINE ETS-1 IN THE SUPERFAMILY OF WINGED HELIX-TURN-HELIX DNA-BINDING PROTEINS},
	journal = {Biochemistry},
	volume = {33},
	number = {46},
	year = {1994},
	note = {ISI Document Delivery No.: PT485Times Cited: 59Cited Reference Count: 46},
	month = {Nov},
	pages = {13509-13516},
	type = {Article},
	abstract = {The members of the ets gene family of transcription factors are characterized by a conserved 85-residue DNA-binding region, termed the ETS domain, that lacks sequence homology to structurally characterized DNA-binding motifs. The secondary structure of the ETS domain of murine Ets-1 was determined on the basis of NMR chemical shifts, NOE and J-coupling constraints, amide hydrogen exchange, circular dichroism, and FT-IR spectroscopy. The ETS domain is composed of three a-helices (H) and four beta-strands (S) arranged in the order H1-S1-S2-H2-H3-S3-S4. The four-stranded antiparallel beta-sheet is the scaffold for a putative helix-turn-helix DNA recognition motif formed by helices 2 and 3. The 25 residues extending beyond the ETS domain to the native C-terminus of the truncated Ets-1 also contain a helical segment. On the basis of the similarity of this topology with that of catabolite activator protein (CAP), heat shock factor (HSF), and hepatocyte nuclear factor (HNF-3 gamma), we propose that ets proteins are members of the superfamily of winged helix-turn-helix DNA-binding proteins.},
	keywords = {3-DIMENSIONAL NMR-SPECTROSCOPY, ASSIGNMENT, BACKBONE AMIDE, COUPLING-CONSTANTS, CRYSTAL-STRUCTURE, LARGER, MOTIF, PROTEINS, SIDE-CHAIN RESONANCES, SPECTRA, TRANSCRIPTION FACTORS},
	isbn = {0006-2960},
	url = {<Go to ISI>://A1994PT48500001},
	author = {Donaldson, L. W. and Petersen, J. M. and Graves, B. J. and McIntosh, L. P.}
}
