@article {2525,
	title = {Detection and assignment of phosphoserine and phosphothreonine residues by C-13-P-31 spin-echo difference NMR spectroscopy},
	journal = {Journal of Biomolecular Nmr},
	volume = {43},
	number = {1},
	year = {2009},
	note = {ISI Document Delivery No.: 379QKTimes Cited: 0Cited Reference Count: 31McIntosh, Lawrence P. Kang, Hyun-Seo Okon, Mark Nelson, Mary L. Graves, Barbara J. Brutscher, Bernhard},
	month = {Jan},
	pages = {31-37},
	type = {Article},
	abstract = {A simple NMR method is presented for the identification and assignment of phosphorylated serine and threonine residues in C-13- or C-13/N-15-labeled proteins. By exploiting modest (similar to 5 Hz) 2- and 3-bond C-13-P-31 scalar couplings, the aliphatic H-1-C-13 signals from phosphoserines and phosphothreonines can be detected selectively in a P-31 spin-echo difference constant time H-1-C-13 HSQC spectrum. Inclusion of the same P-31 spin-echo element within the C-13 frequency editing period of an intraHNCA or HN(CO)CA experiment allows identification of the amide H-1(N) and N-15 signals of residues (i) for which C-13(alpha)(i) or C-13(alpha)(i - 1), respectively, are coupled to a phosphate. Furthermore, P-31 resonance assignments can be obtained by applying selective low power cw P-31 decoupling during the spin-echo period. The approach is demonstrated using a PNT domain containing fragment of the transcription factor Ets-1, phosphorylated in vitro at Thr38 and Ser41 with the MAP kinase ERK2.},
	keywords = {ASSIGNMENT, CENTER-DOT-OP, CONSTANT-TIME, Ets-1, MAP kinase, NUCLEIC-ACIDS, OP HYDROGEN-BONDS, P-31-C-13 scalar coupling, Phosphoprotein, PHOSPHORYLATION, POINTED DOMAIN, PROTEIN, QUANTITATIVE J-CORRELATION, RESONANCE, SCALAR COUPLINGS, TRANSCRIPTION FACTOR},
	isbn = {0925-2738},
	url = {<Go to ISI>://000261411100004},
	author = {McIntosh, L. P. and Kang, H. S. and Okon, M. and Nelson, M. L. and Graves, B. J. and Brutscher, B.}
}
@article {2260,
	title = {Direct observation of the symmetric stretching modes of (A)over-tilde(1) A(u) acetylene by pulsed supersonic jet laser induced fluorescence},
	journal = {Molecular Physics},
	volume = {106},
	number = {15},
	year = {2008},
	note = {ISI Document Delivery No.: 371LATimes Cited: 1Cited Reference Count: 24Steeves, Adam H. Merer, Anthony J. Bechtel, Hans A. Beck, Annelise R. Field, Robert W.},
	pages = {1867-1877},
	type = {Article},
	abstract = {Rotational analyses are reported for the 2(0)(2) and 1(0)(1) bands of the (A) over tilde (1) A(u) <- (X) over tilde (1) Sigma(+)(g) transition of C2H2 near 45,000 cm(-1) (+2800 cm(-1) relative to T-0) from jet-cooled laser-induced fluorescence spectra. While the 220 band is unperturbed and straightforward to assign, the 1(1) level is strongly perturbed by interactions with the 2(1) B-2 polyad, where upsilon B{\textquoteright} = upsilon(4){\textquoteright} + upsilon(6){\textquoteright}. In order to assign the lines of this band, a population-labelling technique was used, employing an infrared laser to deplete the population in selected ground state rotational levels before probing with the ultraviolet laser. Deperturbation of the 1(1)/2(1) B-2 interaction leads to the value v(1){\textquoteright} = 2880.08 cm(-1) for the fundamental symmetric C-H stretching frequency. Assignments are also reported for the 2 3 and 1 1 2 1 levels, completing all assignments of levels containing excitation in only the totally symmetric vibrational modes up to + 4500 cm(-1). The reassignment of upsilon(1){\textquoteright} implies that some of currently accepted assignments above 47,000 cm(-1) are in error and suggests that the interpretation of some aspects of the near-threshold photodissociation measurements of Mordaunt et al. [J. Chem. Phys. 108, 519 (1998)] may need to be revisited.},
	keywords = {AB-INITIO MO, acetylene, ASSIGNMENT, C2H2, DEPERTURBATION, excited states, PARTIAL, PHOTODISSOCIATION, S-1((1)A(U)) STATE, SPECTROSCOPY, vibration-rotation analysis, VIBRATION-ROTATION CONSTANTS, vibrational spectroscopy, WAVELENGTH BANDS, X BAND SYSTEM},
	isbn = {0026-8976},
	url = {<Go to ISI>://000260831600004},
	author = {Steeves, A. H. and Merer, A. J. and Bechtel, H. A. and Beck, A. R. and Field, R. W.}
}
@article {1063,
	title = {Can PISEMA experiments be used to extract structural parameters for mobile beta-barrels?},
	journal = {Journal of Biomolecular Nmr},
	volume = {32},
	number = {2},
	year = {2005},
	note = {ISI Document Delivery No.: 948CRTimes Cited: 4Cited Reference Count: 42},
	month = {Jun},
	pages = {101-111},
	type = {Article},
	abstract = {The effect of mobility on N-15 chemical shift/N-15-H-1 dipolar coupling (PISEMA) solid state NMR experiments applied to macroscopically oriented beta-barrels is assessed using molecular dynamics simulation data of the NalP autotransporter domain embedded in a DMPC bilayer. In agreement with previous findings for alpha-helices, the fast librational motion of the peptide planes is found to have a considerable effect on the calculated PISEMA spectra. In addition, the dependence of the chemical shift anisotropy (CSA) and dipolar coupling parameters on the calculated spectra is evaluated specifically for the beta-barrel case. It is found that the precise choice of the value of the CSA parameters sigma(11), sigma(22) and sigma(33) has only a minor effect, whereas the choice of the CSA parameter theta shifts the position of the peaks by up to 20 ppm and changes the overall shape of the spectrum significantly. As was found for alpha-helices, the choice of the NH bond distance has a large effect on the dipolar coupling constant used for the calculations. Overall, it is found that the alternating beta-strands in the barrel occupy distinct regions of the PISEMA spectra, forming patterns which may prove useful in peak assignment.},
	keywords = {ANGLE-SPINNING NMR, ASSIGNMENT, COAT PROTEIN, CONSTRAINTS, DOMAIN, HELICAL WHEELS, MEMBRANE-PROTEINS, mobility of membrane beta-barrels, MOLECULAR-DYNAMICS SIMULATIONS, mosaic spread, PISEMA, SOLID-STATE NMR, SPECTROSCOPY, time averaging},
	isbn = {0925-2738},
	url = {<Go to ISI>://000230694100001},
	author = {Bleile, D. W. and Scott, W. R. P. and Straus, S. K.}
}
@article {934,
	title = {Diversity in structure and function of the Ets family PNT domains},
	journal = {Journal of Molecular Biology},
	volume = {342},
	number = {4},
	year = {2004},
	note = {ISI Document Delivery No.: 855WLTimes Cited: 17Cited Reference Count: 86},
	month = {Sep},
	pages = {1249-1264},
	type = {Article},
	abstract = {The PNT (or Pointed) domain, present within a subset of the Ets family of transcription factors, is structurally related to the larger group of SAM domains through a common tertiary arrangement of four alpha-helices. Previous studies have shown that, in contrast to the PNT. domain from Tel, this domain from Ets-1 contains an additional N-terminal helix integral to its folded structure. To further investigate the structural plasticity of the PNT domain, we have used NMR spectroscopy to characterize this domain from two additional Ets proteins, Erg and GABPalpha. These studies both define the conserved and variable features of the PNT domain, and demonstrate that the additional N-terminal helix is also present in GABPa, but not Erg. In contrast to Tel and Yan, which self-associate to form insoluble polymers, we also show that the isolated PNT domains from Ets-1, Ets-2, Erg, Fli-1, GABPalpha, and Pnt-P2 are monomeric in solution. Furthermore, these soluble PNT domains do not associate in any pair-wise combination. Thus these latter Ets family PNT domains likely mediate interactions with additional components of the cellular signaling or transcriptional machinery. (C) 2004 Elsevier Ltd. All rights reserved.},
	keywords = {ALPHA-MOTIF SAM, ASSIGNMENT, AUTOMATED, CHEMICAL-SHIFT, DIPOLAR COUPLINGS, ENDOTHELIAL-CELL DIFFERENTIATION, Erg, GABP, GENE, NMR-SPECTRA, POINTED DOMAIN, protein interactions, PROTEIN-KINASE, SAM domain, TRANSCRIPTION FACTOR},
	isbn = {0022-2836},
	url = {<Go to ISI>://000224005500015},
	author = {Mackereth, C. D. and Scharpf, M. and Gentile, L. N. and Macintosh, S. E. and Slupsky, C. M. and McIntosh, L. P.}
}
@article {3819,
	title = {Structural coupling of the inhibitory regions flanking the ETS domain of murine Ets-1},
	journal = {Protein Science},
	volume = {5},
	number = {2},
	year = {1996},
	note = {ISI Document Delivery No.: TU724Times Cited: 46Cited Reference Count: 66},
	month = {Feb},
	pages = {296-309},
	type = {Article},
	abstract = {Several members of the ets gene family of transcription factors show negative regulation of DNA binding by intramolecular interactions. A structural mechanism for this auto-inhibition is investigated using a 161-residue N-terminal deletion mutant of murine Ets-1, Ets-1 Delta N280. This protein shows a similar reduced affinity for DNA as native Ets-1 because it contains the ETS domain in context of the flanking amino- and carboxy-terminal regions that together mediate repression of DNA binding. The secondary structure of Ets-1 Delta N280 was determined using NMR chemical shift, NOE, J coupling, and amide hydrogen exchange information. In addition to the winged helix-turn-helix ETS domain, Ets-1 Delta N280 contains two alpha-helices in the amino-terminal inhibitory region and one alpha-helix in the carboxy-terminal inhibitory region. Chemical shift comparisons were made between this protein and an activated form of Ets-1 lacking the amino-terminal inhibitory region. The spectral differences demonstrate that the amino- and carboxy-terminal inhibitory sequences are structurally coupled to one another, thus explaining the observation that both regions are required for the repression of DNA binding. Furthermore, these data show that the inhibitory sequences also interact directly with the first helix of the intervening ETS domain, thereby providing a pathway for the repression of DNA binding. These results lead to a model of an inhibitory module in Ets-1 composed of both the amino- and carboxy-terminal regions interfaced with the ETS domain. This establishes the structural framework for understanding the intramolecular inhibition of Ets-1 DNA binding.},
	keywords = {3-DIMENSIONAL NMR-SPECTROSCOPY, allosteric, ASSIGNMENT, CRYSTAL-STRUCTURE, DNA binding, DNA-BINDING MOTIF, ETS domain, Ets-1 and Ets-2, FACTORS, H-1, INHIBITION, INTRAMOLECULAR, LARGER PROTEINS, N-15 NMR, NMR, protein structure, SPECTRA, transcription, V-ETS, winged helix-turn-helix},
	isbn = {0961-8368},
	url = {<Go to ISI>://A1996TU72400014},
	author = {Skalicky, J. J. and Donaldson, L. W. and Petersen, J. M. and Graves, B. J. and McIntosh, L. P.}
}
@article {3857,
	title = {Tensor LEED analyses for the (root 3x root 3)R30 degrees and c(4x2) structures formed by sulphur chemisorbed on the (111) surface of rhodium},
	journal = {Surface Science},
	volume = {345},
	number = {1-2},
	year = {1996},
	note = {ISI Document Delivery No.: TT592Times Cited: 17Cited Reference Count: 16},
	month = {Jan},
	pages = {101-109},
	type = {Article},
	abstract = {Tensor LEED analyses have been made for the Rh(111)-(root 3 x root 3)R30 degrees-S and Rh(lll)-c(4 x 2)-S surface structures formed by S chemisorbed at 1/3 and 1/2 monolayer coverages respectively. For the lower-coverage form, S adsorbs on the regular three-coordinate sites which continue the fee packing sequence; the S-Rh bond lengths are indicated to equal 2.23 Angstrom, and relaxations in the metallic structure are negligible. In the c(4 x 2) form, the adsorption occurs equally on both types of three-coordinate site (fee and hcp), although some surface Rh atoms bond to two S atoms while others bond to just one, and this sets up some interesting relaxations. Specifically, the S atoms displace laterally from the centre of the three-fold sites by 0.20 to 0.29 Angstrom, and the first metal layer is buckled by about 0.23 Angstrom. The first-to-second interlayer spacing in the metal expands to 2.26 Angstrom from the bulk value of 2.20 Angstrom. The average S-Rh bond lengths equal 2.22 Angstrom, and so they are not significantly changed from that in the low-coverage form. The structural evolution for S chemisorbed on the (111) surface of rhodium with increasing coverage is compared with the corresponding evolution on the Rh(110) surface.},
	keywords = {ABSORPTION FINE-STRUCTURE, ASSIGNMENT, chalcogens, CRYSTAL SURFACES, HOLLOW ADSORPTION SITE, LOW ENERGY ELECTRON DIFFRACTION (LEED), LOW INDEX SINGLE, NI(111), NO, rhodium, SURFACE RELAXATION},
	isbn = {0039-6028},
	url = {<Go to ISI>://A1996TT59200014},
	author = {Wong, K. C. and Liu, W. and Saidy, M. and Mitchell, K. A. R.}
}
@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.}
}
