@article {2476,
	title = {The ground state rotational spectrum of the fluorosulfate radical},
	journal = {Journal of Chemical Physics},
	volume = {130},
	number = {18},
	year = {2009},
	note = {ISI Document Delivery No.: 448LDTimes Cited: 2Cited Reference Count: 26Kolesnikova, Lucie Varga, Juraj Striteska, Lucie Nova Beckers, Helmut Willner, Helge Aubke, Friedhelm Urban, Stepan},
	month = {May},
	pages = {9},
	type = {Article},
	abstract = {The rotational spectra of the fluorosulfate (FSO3 center dot) molecular radical in its vibronic ground state were measured in the millimeter-wave region and analyzed in detail using the matrix elements of the rotational, fine, and hyperfine Hamiltonian terms. The analysis of the assigned transition frequencies made it possible to derive very precise values of the rotational, centrifugal distortion and fine structure constants and to confirm the C-3v molecular symmetry of the vibronic ground state unambiguously. In addition, an effective parameter of the "A(1)-A(2) splitting" was determined. The rotational transitions of the FSO3 center dot free radical were observed, identified, and analyzed for the first time.},
	keywords = {ASSIGNMENTS, BANDS, CLASSIFICATION, fluorine compounds, free radical reactions, ground states, HYPERFINE, LASER EXCITATION, lifetimes, millimetre wave spectra, molecular configurations, radiative, rotational states, STRUCTURE, SYMMETRIC-TOP MOLECULES, SYSTEM, vibronic states},
	isbn = {0021-9606},
	url = {<Go to ISI>://000266263200023},
	author = {Kolesnikova, L. and Varga, J. and Striteska, L. N. and Beckers, H. and Willner, H. and Aubke, F. and Urban, S.}
}
@article {713,
	title = {Characterizing the pH-dependent stability and catalytic mechanism of the family 11 xylanase from the alkalophilic Bacillus agaradhaerens},
	journal = {Carbohydrate Research},
	volume = {338},
	number = {5},
	year = {2003},
	note = {ISI Document Delivery No.: 645XBTimes Cited: 6Cited Reference Count: 38},
	month = {Feb},
	pages = {415-421},
	type = {Article},
	abstract = {The xylanase, BadX, from the alkalophilic Bacillus agaradhaerens was cloned, expressed and studied in comparison to a related family 11 xylanase, BcX, from B. circulans. Despite the alkaline versus neutral conditions under which these bacteria grow, BadX and BcX both exhibit optimal activity near pH 5.6 using the substrate omicron-nitrophenyl beta-xylobioside. Analysis of the bell-shaped activity profile of BadX yielded apparent pK(a) values of 4.2 and 7.1, assignable to its nucleophile Glu94 and general acid Glu184, respectively. In addition to having an similar to 10-fold higher k(cat)/K-m value with this substrate at pH 6 and 40 degreesC, BadX has significantly higher thermal stability than BcX under neutral and alkaline conditions. This enhanced stability, rather than a shift in its pH-optimum, may allow BadX to hydrolyze xylan under conditions of elevated temperature and pH. (C) 2003 Elsevier Science Ltd. All rights reserved.},
	keywords = {bacillus xylanase, CIRCULANS XYLANASE, CLASSIFICATION, electrostatic, extremophile, glycosidase, GLYCOSYL-ENZYME INTERMEDIATE, HYDROLASES, interactions, NMR ASSIGNMENTS, pH-dependent mechanism, PK(A), PROTEIN, STABILITY, THERMOSTABILITY},
	isbn = {0008-6215},
	url = {<Go to ISI>://000181004800004},
	author = {Poon, D. K. Y. and Webster, P. and Withers, S. G. and McIntosh, L. P.}
}
@article {4772,
	title = {Structural proteomics of an archaeon},
	journal = {Nature Structural Biology},
	volume = {7},
	number = {10},
	year = {2000},
	note = {ISI Document Delivery No.: 362LRTimes Cited: 188Cited Reference Count: 29},
	month = {Oct},
	pages = {903-909},
	type = {Article},
	abstract = {A set of 424 nonmembrane proteins from Methanobacterium thermoautotrophicum were cloned, expressed and purified for structural studies. Of these, similar to 20\% were found to be suitable candidates for X-ray crystallographic or NMR spectroscopic analysis without further optimization of conditions, providing an estimate of the number of the most accessible structural targets in the proteome. A retrospective analysis of the experimental behavior of these proteins suggested some simple relations between sequence and solubility. implying that data bases of protein properties will be useful in optimizing high throughput strategies. Of the first 10 structures determined, several provided clues to biochemical functions that were not detectable from sequence analysis, and in many cases these putative functions could be readily confirmed by biochemical methods. This demonstrates that structural proteomics is feasible and can play a central role in functional genomics},
	keywords = {ALIGNMENT, CLASSIFICATION, GENE, genomics, PREDICTION, PROTEIN-STRUCTURE, SCOP},
	isbn = {1072-8368},
	url = {<Go to ISI>://000089779900022},
	author = {Christendat, D. and Yee, A. and Dharamsi, A. and Kluger, Y. and Savchenko, A. and Cort, J. R. and Booth, V. and Mackereth, C. D. and Saridakis, V. and Ekiel, I. and Kozlov, G. and Maxwell, K. L. and Wu, N. and McIntosh, L. P. and Gehring, K. and Kennedy, M. A. and Davidson, A. R. and Pai, E. F. and Gerstein, M. and Edwards, A. M. and Arrowsmith, C. H.}
}
@article {4197,
	title = {Mechanisms of cellulases and xylanases},
	journal = {Biochemical Society Transactions},
	volume = {26},
	number = {2},
	year = {1998},
	note = {ISI Document Delivery No.: ZT170Times Cited: 22Cited Reference Count: 24664th Meeting of the Biochemical-SocietyDEC 15-17, 1997READING, ENGLANDBiochem Soc},
	month = {May},
	pages = {156-160},
	type = {Proceedings Paper},
	keywords = {ACID-SEQUENCE SIMILARITIES, ACTIVE-SITE, BACILLUS-CIRCULANS XYLANASE, CLASSIFICATION, ENZYME, FAMILIES, GLUCOSIDASE, glycosidase, GLYCOSYL HYDROLASES, HYDROLYSIS, nucleophile},
	isbn = {0300-5127},
	url = {<Go to ISI>://000074056400019},
	author = {Birsan, C. and Johnson, P. and Joshi, M. and MacLeod, A. and McIntosh, L. and Monem, V. and Nitz, M. and Rose, D. R. and Tull, D. and Wakarchuck, W. W. and Wang, Q. and Warren, R. A. J. and White, A. and Withers, S. G.}
}
