This is an interview conducted with an oil and gas worker who was employed in the industry from 1993 to 2012. He requested that his name not be used. From 2008 to 2012, he drilled wells for a major operator in Bradford County, Pennsylvania. Bradford County is the center of the Marcellus shale gas boom in Northeastern Pennsylvania. In 2012, he formed a consulting business to assist clients who need information on the details of gas and oil drilling operations. In this interview, the worker describes the benefits and difficulties of the hard work involved in drilling unconventional gas wells in Pennsylvania. In particular, he outlines the safety procedures that were in place and how they sometimes failed, leading to workplace injuries. He provides a compelling view of the trade-offs between the economic opportunities of working on a rig and the dangers and stresses of working long hours under hazardous conditions.

Low cost manufacturing of Cu(In,Ga)Se2 (CIGS) films for high efficiency PV devices by the innovative Field-Assisted Simultaneous Synthesis and Transfer (FASST®) process is reported. The FASST® process is a two-stage reactive transfer printing method relying on chemical reaction between two separate precursor films to form CIGS, one deposited on the substrate and the other on a printing plate in the first stage. In the second stage these precursors are brought into intimate contact and rapidly reacted under pressure in the presence of an applied electrostatic field. The method utilizes physical mechanisms characteristic of anodic wafer bonding and rapid thermal annealing, effectively creating a sealed micro-reactor that insures high material utilization efficiency, direct control of reaction pressure, and low thermal budget. The use of two independent precursors provides the benefits of independent composition and flexible deposition technique optimization, and eliminates pre-reaction prior to the second stage FASST® synthesis of CIGS. High quality CIGS with large grains on the order of several microns are formed in just several minutes based on compositional and structural analysis by XRF, SIMS, SEM and XRD. Cell efficiencies of 12.2% have been achieved using this method.

Stationary points of the potential surface for the S(N)2 reaction F-+CH3Cl-->FCH3+Cl- have been investigated by large-scale CCSD(T) calculations. The ion-dipole complexes in the reactant and product channels have well depths of 15.8 and 9.6 kcal mol(-1), respectively, and are separated by a small barrier of 3.3 +/- 0.3 kcal mol(-1). The molar reaction enthalpy at 298 K is obtained to be -31.5 kcal mol(-1).

The vibrational structure of the first bands of the photoelectron (PE) spectra of the radicals SiH 3 , CF 3 , CH 2 CN and CH 2 NC has been calculated by means of the Coupled Electron Pair Approximation. Excellent agreement with experiment is obtained for SiH 3 . A long progression in the umbrella bending vibration is calculated for CF 3 . Furthermore, two combination tone series should be observable in the PE spectrum at higher resolution. The PE spectra of CH 2 CN and CH 2 NC are dominated by the adiabatic peaks. Adiabatic ionization potentials of 8.98±0.05 eV, 10.20±0.05 eV and 9.36±0.03 eV are predicted for CF 3 , CH 2 CN and CH 2 NC.

Neurons from rat superior cervical ganglia were grown in coculture with pineal cells. Action potentials of neurons in cocultures were 25% longer and were 25% greater in amplitude than those recorded from neurons grown in the presence of ganglionic nonneuronal cells alone.

The effects of three allosteric ligands of the acetylcholine receptor (tetracaine, (-)N-allylnormetazocine [ANMC, SKF-10047], and phencyclidine [PCP]) on the single channel currents of the nicotinic acetylcholine receptor (AChR) of BC3H-1 cells obtained from the American Type Culture Association were examined. At micromolar concentrations these agents acted as noncompetitive blockers of acetylcholine (ACh) activated currents. In the presence of ACh alone, the distributions of apparent open times and burst durations were fit by double exponential functions: τ1=.46 ±.03 ms, τ2 = 14.4 ±.9 ms for the open time distributions, and τ1=.45 ±.02 ms, τ2 = 15.5 ± 1.2 ms for burst durations. The relative area of the distributions represented by the short duration events decreased as a function of the concentration of ACh, representing 71 ± 3% of the area at 20 nM ACh and only 26 ± 8% at 2 µM ACh for the open time distributions. In the presence of 100 nM ACh, tetracaine, PCP, and ANMC decreased apparent mean channel open times with IC50 ’s of 2.5 ±.5 µM, 5.0 ±.5µM, and 3.0 ±.5µM, respectively. The effects of tetracaine were inconsistent with a model for sequential block of open channels. The number of fast closures decreased in the presence of increasing concentrations of tetracaine, and the ratio of long and short events remained constant at all concentrations of tetracaine. This suggests that, in the presence of tetracaine, events were more likely to occur in isolation and that, at concentrations which more effectively blocked long duration events, the channel was not required to pass through the same open state repeatedly in order to return to the normal closed state. In addition, tetracaine acted as an agonist at concentration greater than 75 µM. In the presence of ANMC, in the range of concentration near the IC50 for the block of long events, the ratio of long to short events increased substantially. ANMC also introduced a new component into the distribution of closed times, τ=13 ms. The area represented by this component increased with the concentration of ANMC and may represent the time that the channel is blocked by ANMC. The effects of ANMC seem more consistent with a mechanism of sequential block. Block by PCP also influenced the ratios of long and short events. A new component of the closed time distributions appeared that was several seconds long and increased with increasing concentration of PCP. In conclusion, we distinguish two types of channel block with these ligands: one consistent with sequential block of open channels and another which may allow the channel to pass into other state during the block.

3H chlorpromazine binds to acetylcholine receptor-rich membrane fragments prepared from Torpedo marmorata electric organ in three different manners: (1) at the level of high affinity sites from which it is displaced by perhydrohistrionicotoxin, (2) at the level of low affinity sites insensitive to this toxin, and (3) in a non saturable manner to a presumably lipidic phase. Binding of chlorpromazine to the first two categories of sites independently stabilizes the "desensitized" high affinity state of the receptor for cholinergic agonists. There exists one high affinity site per two snake alpha-toxin sites, thus per 250,000 daltons light form of the receptor. Under the conditions of 3H chlorpromazine high affinity binding, ultraviolet irradiation results in the covalent incorporation of this ligand to the four chains of the receptor.

Reversible ligands were attached covalently to membrane-bound acetylcholine receptor from Torpedo marmorata by a method which is generally applicable and does not require the synthesis of specially designed molecules. UV irradiation of the receptor in the presence of [3H]trimethisoquin, [3H]phencyclidine, or [3H]perhydrohistrionicotoxin resulted in the labeling of the binding site(s) for these noncompetitive blockers of the permeability response. The labeling of the delta chain was enhanced by carbamoylcholine, and this increase was blocked by snake alpha-toxins. The effect of carbamoylcholine on [3H]trimethisoquin binding was more pronounced than with the other two noncompetitive blockers; in all instances, the labeling was abolished by unlabeled histrionicotoxin. These three compounds therefore interact with the high-affinity site for noncompetitive blockers. Incorporation of radioactivity also occurred into the alpha chain but either was insensitive to cholinergic effectors or decreased in the presence of carbamoylcholine (or snake alpha-toxin), probably as a result of an interaction with the acetylcholine-binding site. In contrast to the other noncompetitive blockers tested, [3H]chlorpromazine heavily labeled the four receptor polypeptides (alpha, beta, gamma, delta), and this labeling also was enhanced by carbamoylcholine and decreased by histrionicotoxin. These data indicate a contribution of the delta chain to the binding site(s) of several well-characterized noncompetitive blockers and suggest that other receptor polypeptides may also contribute to this binding.

The 66 000-dalton or delta subunit of the acetylcholine receptor from Torpedo marmorata was covalently labeled in the presence of carbamoylcholine by 5-azido [3H]trimethisoquin (5-A[3H]T), a photoaffinity derivative of the local anesthetic trimethisoquin. After the attack of purified receptor with increasing concentrations of trypsin, the delta chain successively yielded fragments with apparent molecular weights of 50 000 (distinct from the beta subunit and referred to as the 50 000-bis (fragment), 49 000, and 47 000. With nondenatured (sodium cholate solubilized or membrane-bound) receptor, the 47 000-dalton fragment was not sensitive to trypsin and contained all of the covalent 5-A[3H]T label. This fragment was still glycosylated and had the same amino acid N terminus, valine, as the intact delta chain. A specific in vitro phosphorylation site of the delta subunit was located between the 49 000- and 50 000-dalton trypsin cleavage fragment and most likely is exposed to the cytoplasmic side of the membrane. A 16 000-dalton fragment of the delta chain was identified, which carriers a disulfide bond (or bonds) capable of cross-linking nonreduced receptor 9S monomerse into 12S dimers. The fragment did not remain associated with the receptor molecule after trypsin treatment.

FEBS LettersVolume 116, Issue 1 p. 30-36 Full-length articleFree Access Conditions for the selective labelling of the 66 000 dalton chain of the acetylcholine receptor by the covalent non-competitive blocker 5-azido-[3H]trimethisoquin Tsunao Saitoh, Tsunao Saitoh Neurobiologie Moléculaire et Laboratoire Associé au Centre National de la Recherche Scientifique, Interactions Moléculaires et Cellulaires, Institut Pasteur, Paris, FranceSearch for more papers by this authorRobert Oswald, Robert Oswald Neurobiologie Moléculaire et Laboratoire Associé au Centre National de la Recherche Scientifique, Interactions Moléculaires et Cellulaires, Institut Pasteur, Paris, FranceSearch for more papers by this authorLawrence P. Wennogle, Lawrence P. Wennogle Neurobiologie Moléculaire et Laboratoire Associé au Centre National de la Recherche Scientifique, Interactions Moléculaires et Cellulaires, Institut Pasteur, Paris, FranceSearch for more papers by this authorJean-Pierre Changeux, Jean-Pierre Changeux Neurobiologie Moléculaire et Laboratoire Associé au Centre National de la Recherche Scientifique, Interactions Moléculaires et Cellulaires, Institut Pasteur, Paris, FranceSearch for more papers by this author Tsunao Saitoh, Tsunao Saitoh Neurobiologie Moléculaire et Laboratoire Associé au Centre National de la Recherche Scientifique, Interactions Moléculaires et Cellulaires, Institut Pasteur, Paris, FranceSearch for more papers by this authorRobert Oswald, Robert Oswald Neurobiologie Moléculaire et Laboratoire Associé au Centre National de la Recherche Scientifique, Interactions Moléculaires et Cellulaires, Institut Pasteur, Paris, FranceSearch for more papers by this authorLawrence P. Wennogle, Lawrence P. Wennogle Neurobiologie Moléculaire et Laboratoire Associé au Centre National de la Recherche Scientifique, Interactions Moléculaires et Cellulaires, Institut Pasteur, Paris, FranceSearch for more papers by this authorJean-Pierre Changeux, Jean-Pierre Changeux Neurobiologie Moléculaire et Laboratoire Associé au Centre National de la Recherche Scientifique, Interactions Moléculaires et Cellulaires, Institut Pasteur, Paris, FranceSearch for more papers by this author First published: July 14, 1980 https://doi.org/10.1016/0014-5793(80)80522-9Citations: 91AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat References 1 T. Heidmann, J.P. Changeux, Ann. Rev. Biochem., 47, (1978), 371– 441. 2 A. Karlin, G. Poste Cell Surface Reviews 6, (1980), Elsevier/North-Holland Amsterdam, New York in press 3 F.J. Barrantes, Ann. Rev. Biophys. Bioeng., 8, (1979), 287– 321. 4 J.P. Changeux, T. Podleski, L. Wofsy, Proc. Natl. Acad. Sci. USA, 58, (1967), 2063– 2070. A. Karlin, M. Winnik, Proc. Natl. Acad. Sci. USA, 60, (1968), 668– 674. 5 A. Sobel, M. Weber, J.P. Changeux, Eur. J. Biochem., 80, (1977), 215– 224. 6 V. Witzemann, M.A. Raftery, Biochemistry, 16, (1978), 5862– 5868. 7 V. Damle, M. McLaughlin, A. Karlin, Biochem. Biophys. Res. Commun., 84, (1978), 845– 851. 8 V.N. Damle, A. Karlin, Biochemistry, 17, (1978), 2039– 2045. 9 E. Weiland, D. Frisman, P. Taylor, Mol. Pharmacol., 15, (1979), 213– 226. 10 H. Moore, M.A. Raftery, Biochemistry, 18, (1979), 1862– 1867. 11 A. Devillers-Thiéry, J.P. Changeux, P. Paroutaud, A.D. 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FEBS LettersVolume 111, Issue 1 p. 29-34 Full-length articleFree Access Selective labelling by [3H]trimethisoquin azide of polypeptide chains present in acetylcholine receptor-rich membranes from Torpedo marmorata Robert Oswald, Robert Oswald Neurobiologie Moléculaire et Laboratoire associé au Centre National de la Recherche Scientifique, Interactions moléculaires et cellulaires, Institut Pasteur, Paris, FranceSearch for more papers by this authorAndré Sobel, André Sobel Neurobiologie Moléculaire et Laboratoire associé au Centre National de la Recherche Scientifique, Interactions moléculaires et cellulaires, Institut Pasteur, Paris, FranceSearch for more papers by this authorGilles Waksman, Gilles Waksman UER des Sciences Pharmaceutiques et Biologiques, Département de Chimie Organique ERA 613 (CNRS), 4, avenue de l'Observatoire, 75270 Paris Cedex 06, FranceSearch for more papers by this authorBernard Roques, Bernard Roques UER des Sciences Pharmaceutiques et Biologiques, Département de Chimie Organique ERA 613 (CNRS), 4, avenue de l'Observatoire, 75270 Paris Cedex 06, FranceSearch for more papers by this authorJean-Pierre Changeux, Jean-Pierre Changeux Neurobiologie Moléculaire et Laboratoire associé au Centre National de la Recherche Scientifique, Interactions moléculaires et cellulaires, Institut Pasteur, Paris, FranceSearch for more papers by this author Robert Oswald, Robert Oswald Neurobiologie Moléculaire et Laboratoire associé au Centre National de la Recherche Scientifique, Interactions moléculaires et cellulaires, Institut Pasteur, Paris, FranceSearch for more papers by this authorAndré Sobel, André Sobel Neurobiologie Moléculaire et Laboratoire associé au Centre National de la Recherche Scientifique, Interactions moléculaires et cellulaires, Institut Pasteur, Paris, FranceSearch for more papers by this authorGilles Waksman, Gilles Waksman UER des Sciences Pharmaceutiques et Biologiques, Département de Chimie Organique ERA 613 (CNRS), 4, avenue de l'Observatoire, 75270 Paris Cedex 06, FranceSearch for more papers by this authorBernard Roques, Bernard Roques UER des Sciences Pharmaceutiques et Biologiques, Département de Chimie Organique ERA 613 (CNRS), 4, avenue de l'Observatoire, 75270 Paris Cedex 06, FranceSearch for more papers by this authorJean-Pierre Changeux, Jean-Pierre Changeux Neurobiologie Moléculaire et Laboratoire associé au Centre National de la Recherche Scientifique, Interactions moléculaires et cellulaires, Institut Pasteur, Paris, FranceSearch for more papers by this author First published: February 25, 1980 https://doi.org/10.1016/0014-5793(80)80754-XCitations: 39AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat References 1 J.B. Cohen, M. Weber, M. Huchet, J.P. Changeux, FEBS Lett., 26, (1972), 43– 47. 2 J.R. Duguid, M.A. Raftery, Arch. Biochem. Biophys., 159, (1973), 512– 516. 3 A. Sobel, M Weber, J.P. Changeux, Eur. J. Biochem., 80, (1977), 215– 224. 4 T. Heidmann, J.P. Changeux, Ann. Rev. Biochem., 47, (1978), 371– 441. 5 M.A. Raftery, R.L. Vandlen, K.L. Reed, T. Lee, Cold Spring Harbor Symp. Quant. Biol., 40, (1976), 193– 202. 6 S.D. Flanagan, S.H. Barondes, R. Taylor, J. Biol. Chem., 251, (1976), 858– 865. 7 J.P. Changeux, T. Podleski, L. Wofsy, Proc. Natl. Acad. Sci. USA, 58, (1967), 2063– 2070. G. Weiland, D. Frisman, P. Taylor, Mol. Pharmacol., 15, (1979), 213– 226. 8 V.N. Damle, A. Karlin, Biochemistry, 17, (1978), 2039– 2045. 9 V.N. Damle, M. McLaughlin, A. Karlin, Biochem. Biophys. Res. Commun., 84, (1978), 845– 853. 10 H.P. Moore, M.A. Raftery, Biochemistry, 18, (1979), 1862– 1867. 11 V. Witzemann, M.A. Raftery, Biochemistry, 16, (1978), 5862– 5868. 12 M. Raftery, S. Blanchard, J. Elliott, P. Hartig, H.-P. Moore, Y. Quast, M. Schimerlik, V. Witzemann, W. Wu, Adv. Cytopharmacol., 3, (1979), 159– 182. 13 A. Sobel, T. Heidmann, J. Hofler, J.P. Changeux, Proc. Nat. Acad. Sci. USA, 75, (1978), 510– 514. 14 J.P. Changeux, T. Heidmann, J.L. Popot, A. Sobel, FEBS Lett., 105, (1979), 181– 187. 15 A. Sobel, T. Heidmann, J. Cartaud, J.P. Changeux, Eur. J. Biochem., (1980), submitted 16 S.G. Blanchard, M.A. Raftery, Proc. Natl. Acad. Sci. USA, 76, (1979), 81– 85. 17 R.R. Neubig, E.K. Krodel, N.D. Boyd, J.B. Cohen, Proc. Natl. Acad. Sci. USA, 76, (1979), 690– 694. 18 A. Karlin, V. Damle, S. Hamilton, M. McLaughlin, R. Valderama, D. Wise, Adv. Cytopharmacol., 3, (1979), 183– 189. 19 V. Witzemann, M.A. Raftery, Biochem. Biophys. Res. Commun., 85, (1978), 623– 631. 20 L.P. Wennogle, J.P. Changeux, Eur. J. Biochem., (1980), in press 21 G. Waksman, R. Oswald, J.P. Changeux, B. Roques, FEBS Lett., 111, (1980), 23– 28. 22 E. Krodel, R.A. Beckman, J.B. Cohen, Mol. Pharmacol., 15, (1979), 294– 312. 23 T. Heidmann, A. Sobel, J.P. Changeux, FEBS Lett., 94, (1978), 397– 404. 24 T. Heidmann, A. Sobel, J.L. Popot, J.P. Changeux, Eur. J. Biochem., (1980), submitted 25 A. Maelicke, B.W. Fulpius, R.P. Klett, E. Reich, J. Biol. Chem., 252, (1977), 4811– 4830. 26 W.M. Bonner, R.L. Laskey, Eur. J. Biochem., 46, (1974), 83– 88. 27 P.H. O'Farell, J. Biol. Chem., 250, (1975), 4007– 4021. 28 M. Weber, J.P. Changeux, Mol. Pharmacol., 10, (1974), 35– 40. 29 J.B. Cohen, M. Weber, J.P. Changeux, Mol. Pharmacol., 10, (1974), 904– 932. 30 H. Sigiyama, J.P. Changeux, Eur J. Biochem., 55, (1975), 505– 515. 31 H.H. Grünhagen, M. Iwatsubo, J.P. Changeux, Eur. J. Biochem., 80, (1977), 225– 240. 32 G. Kato, J.P. Changeux, Mol. Pharmacol., 12, (1976), 92– 100. 33 A.T. Eldefrawi, M.E. Eldefrawi, E.X. Albuquerque, A.C. Oliveira, N. Mansour, M. Adler, J.W. Daly, G.B. Brown, W. Burgemeister, B. Witkop, Proc. Natl. Acad. Sci. USA, 74, (1977), 2172– 2176. 34 F. Hucho, FEBS Lett., 103, (1979), 27– 32. Citing Literature Volume111, Issue1February 25, 1980Pages 29-34 ReferencesRelatedInformation

FEBS LettersVolume 111, Issue 1 p. 23-28 Full-length articleFree Access Synthesis and pharmacological activity on Electrophorus electricus electroplaque of photoaffinity labelling derivatives of the non-competitive blockers di- and tri-methisoquin Gilles Waksman, Gilles Waksman Département de Chimie Organique, ERA 613 (CNRS), UER des Sciences Pharmaceutiques et Biologiques, 4 avenue de l'Observatoire, 75270 Paris Cedex 06 FranceSearch for more papers by this authorRobert Oswald, Robert Oswald Neurobiologie Moléculaire et Laboratoire associé au Centre National de la Recherche Scientifique, Interactions Moléculaires et Cellulaires, Institut Pasteur, 25 rue du Docteur Roux, 75015 Paris, FranceSearch for more papers by this authorJean-Pierre Changeux, Jean-Pierre Changeux Neurobiologie Moléculaire et Laboratoire associé au Centre National de la Recherche Scientifique, Interactions Moléculaires et Cellulaires, Institut Pasteur, 25 rue du Docteur Roux, 75015 Paris, FranceSearch for more papers by this authorBernard P. Roques, Bernard P. Roques Département de Chimie Organique, ERA 613 (CNRS), UER des Sciences Pharmaceutiques et Biologiques, 4 avenue de l'Observatoire, 75270 Paris Cedex 06 FranceSearch for more papers by this author Gilles Waksman, Gilles Waksman Département de Chimie Organique, ERA 613 (CNRS), UER des Sciences Pharmaceutiques et Biologiques, 4 avenue de l'Observatoire, 75270 Paris Cedex 06 FranceSearch for more papers by this authorRobert Oswald, Robert Oswald Neurobiologie Moléculaire et Laboratoire associé au Centre National de la Recherche Scientifique, Interactions Moléculaires et Cellulaires, Institut Pasteur, 25 rue du Docteur Roux, 75015 Paris, FranceSearch for more papers by this authorJean-Pierre Changeux, Jean-Pierre Changeux Neurobiologie Moléculaire et Laboratoire associé au Centre National de la Recherche Scientifique, Interactions Moléculaires et Cellulaires, Institut Pasteur, 25 rue du Docteur Roux, 75015 Paris, FranceSearch for more papers by this authorBernard P. Roques, Bernard P. Roques Département de Chimie Organique, ERA 613 (CNRS), UER des Sciences Pharmaceutiques et Biologiques, 4 avenue de l'Observatoire, 75270 Paris Cedex 06 FranceSearch for more papers by this author First published: February 25, 1980 https://doi.org/10.1016/0014-5793(80)80753-8Citations: 17AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat References 1 T. Heidmann, J.P. Changeux, Ann. Rev. Biochem., 47, (1978), 317– 357. 10.1146/annurev.bi.47.070178.001533 CASPubMedWeb of Science®Google Scholar 2 C.Y. Lee, Ann. 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