@article {3774,
	title = {Microwave Fourier transform spectroscopy of perchloryl fluoride: (FClO3)-F-19-Cl-35/37-O-16 and (FClO2O)-F-19-Cl-35/37-O-16-O-18},
	journal = {Journal of Molecular Spectroscopy},
	volume = {175},
	number = {1},
	year = {1996},
	note = {ISI Document Delivery No.: TX208Times Cited: 18Cited Reference Count: 81},
	month = {Jan},
	pages = {120-132},
	type = {Article},
	abstract = {O-18-enriched, monolabeled perchloryl fluoride, (FClO2O)-F-19-Cl-35/37-O-16-O-18, has been synthesized. Its rotational spectrum has been studied in the 4-22 GHz region. In addition, the spectra of the symmetric isotopomers (FClO3)-F-19-Cl-35/37-O-16 have been reinvestigated. Rotational and centrifugal distortion constants, as well as chlorine nuclear quadrupole and chlorine and fluorine spin-rotation and spin-spin coupling constants, have been determined for the ground vibrational state. The ground state rotational data have been used to evaluate geometrical parameters. The harmonic force field has been refined. The results are compared with data of related molecules. (C) 1996 Academic Press. Inc.},
	keywords = {BANDS, BOND LENGTHS, COUPLING-CONSTANTS, FCLO3, FORCE-CONSTANTS, N-F, NU-2, ROTATIONAL SPECTRUM, SPECTROMETER, STATES},
	isbn = {0022-2852},
	url = {<Go to ISI>://A1996TX20800017},
	author = {Muller, H. S. P. and Gerry, M. C. L.}
}
@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 {3657,
	title = {Solution structure of the ETS domain from murine Ets-1: A winged helix-turn-helix DNA binding motif},
	journal = {Embo Journal},
	volume = {15},
	number = {1},
	year = {1996},
	note = {ISI Document Delivery No.: TQ160Times Cited: 113Cited Reference Count: 68},
	month = {Jan},
	pages = {125-134},
	type = {Article},
	abstract = {Ets-1 is the prototypic member of the ets family of transcription factors, This family is characterized by the conserved ETS domain that mediates specific DNA binding, Using NMR methods, we have determined the structure of a fragment of murine Ets-1 composed of the 85 residue ETS domain and a 25 amino acid extension that ends at its native C-terminus. The ETS domain folds into a helix-turn-helix moth on a four-stranded anti-parallel beta-sheet scaffold. This structure places Ets-1 in the winged helix-turn-helix (wHTH) family of DNA binding proteins and provides a model for interpreting the sequence conservation of the ETS domain and the specific interaction of Ets-1 with DNA. The C-terminal sequence of Ets-1, which is mutated in the v-Ets oncoprotein, forms an alpha-helix that packs anti-parallel to the N-terminal helix of the ETS domain, In this position, the C-terminal helix is poised to interact directly with an N-terminal inhibitory region in Ets-1 as well as the wHTH motif. This explains structurally the concerted role of residues flanking the ETS domain in the intramolecular inhibition of Ets-1 DNA binding.},
	keywords = {AMINO-ACID SUBSTITUTION, C-13, C-ETS-1, COUPLING-CONSTANTS, CRYSTAL-STRUCTURE, DNA binding, ERYTHROBLASTOSIS, FACTORS, GENE FAMILY, intramolecular inhibition, protein NMR structure, PROTEINS, selective labelling, transcription, V-ETS, winged helix-turn-helix},
	isbn = {0261-4189},
	url = {<Go to ISI>://A1996TQ16000013},
	author = {Donaldson, L. W. and Petersen, J. M. and Graves, B. J. 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.}
}
