xt76ww76wr7x https://nyx.uky.edu/dips/xt76ww76wr7x/data/mets.xml University of Kentucky University of Kentucky Chemistry Department 20060331 A brochure for the Naff Symposium, an event hosted by the University of Kentucky Chemistry Department supported by the Anna S. Naff Endowment Fund. This brochure belongs to the University of Kentucky Chemistry Department Records collection, accession number 2014ua075. archival material  English University of Kentucky Chemistry Department Contact the Special Collections Research Center for information regarding rights and use of this collection. University of Kentucky Chemistry Department Naff Symposium brochures Thirty-Second Annual Symposium on Chemistry and Molecular Biology: "Mass Spectrometry of Biological Systems" text Thirty-Second Annual Symposium on Chemistry and Molecular Biology: "Mass Spectrometry of Biological Systems" 2006 2017 true xt76ww76wr7x section xt76ww76wr7x M4,, gr 1 gangasfi-gs; " rr§2,,.~,“_f’r_ '33.»? ”48 ~ g:ti:n~;,~‘”were; Manger-12g : km. 3“ M. L»- -7 w M r4 2’ ”:- ' r’s- M,,.-*~M r, :' M-z: - “w“: 4. Mt. 1‘ r. 2 J v; . . 2 .
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microns In diameter and typically COVeTS the m/z range 1000‘ Technologies and methods of proteomics will be described fitiftfit . _ $3,: $2.1; ,‘
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corresponding normal tissue. This will be illustrated with stud- "Biological Mass Spectrometry: Metabolom- > L0 3‘ t 3,3" axis}; _————_— 3' ‘75 33%!
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and biopsy specimens. Imaging MS has also been applied to :Iefitr%sprayhionization (.D Sf )' his method '5 shown to allow 0 5 q- é.“ 3:., Richard M Ca HO“ 5" {3’1 3‘
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I _ _ , ,3: 3523
3 Department of Chemistry, Unrversrty of Kentucky twin,
3.3,
:3 presents the i333.‘
i :i first"? i"? ' ”45‘
3 Thirty-Second Annual Naff Symposrum on 3,3»
hemistry & 3.,
' tr
o ecular Biology m...
3 established In the memory of Anna S. Naff *3“ r;
" l 3:“ .t”-w,,“:~_-',} 1:", 452-7
3 Friday, March 31, 2006 9:00 am. 323:3
. . . I . r ~."-',"°z,='!;_’. ”,3,‘
3 William T. Young Library Auditorium jg;
—____________—__________._____ 3
' l l "(3": ‘1 \f. ruffle;
3 Mass Spectrometry of Biological Systems
ii Iii-‘5‘"; ‘ r.
3 53333:? _ 3 Richard M. Caprioli, Stanley Cohen Professor of Biochemistry, Director of the Mass Spec- ,~»-~:§f
3 fl ’ - trometry Research Center, Professor, Departments of Chemistry and Pharmacology, Vander- 33,: 223135-8333:
3 ,_;'~«‘" ' - - bilt University School of Medicine. Dr. Caprioli received his BS. in 1965 from Columbia University 'i,"%?fgé;:,,h
i3 . ,. ‘ ' a .. in New York, NY, his PhD. in 1969 in Biochemistry, also at Columbia University with Professor David 33:13:13??? f?
31, 33:, ‘ ~ ‘ ,_ Rittenberg. He did a one-year postdoctoral fellowship at Purdue University with Professor John H. f‘afia‘
33’ 3533;? Beynon. In 1970, he was appointed as Assistant Professor of Biochemistry at Purdue. In 1975, Dr. 2,:“ ”39%.:
3‘3 " 33233 2" . Caprioli moved to the University of Texas Medical School in Houston where he was Professor of Bio- mags?“
3 " chemistry and Molecular Biology and Director of the Analytical Chemistry Center until his move to 3321-273?“ ”3‘
3 _I ‘ Nashville in early 1998. Professor Caprioli is interested in the use of mass spectrometry for the 3¢fififiéti
3 \ , ‘ e' ' j analysis of compounds in biological systems. Current work includes the use of electrospray and la- "iv 37* fig
;’, (3‘ ser desorption ionization methods with biological tissues and samples. Applications have focused on éfgxww '. 1‘ ,
:3 the development of this instrumentation and associated methodologies to achieve ultra-high sensitivity detection of en- 3:37;,”3u
3‘3 dogenous compounds (e.g., neuropeptides) in live animal systems. He has published over 300 scientific papers, including Eggjggeffugasf-
33 three books. Recent work involves the development of Imaging Mass Spectrometry, a technique whereby molecular im- «:v f"% ‘i
3 ages of peptides, proteins, drugs and other compounds are localized in tissue sections with molecular weight specificity. ,‘xfiffisg
'i This method involves molecular mapping of animal tissue through the production of ion images obtained from the analysis 3 ”5"
3 of mammalian tissue. Applications to specific research areas involve questions about certain spatial distributions of mole- imgfifi’é:
cl cules within specific tissues, e.g., mapping proteins in cancer tissue. Specific applications include human glioblastomas, 153' 32*"...
g aberrant mouse colon crypts, and mouse prostate tumors. Dr. Caprioli has been a member of the American Society for $33th 33:
6* Mass Spectrometry since 1975; he recently served two years each as President of the Society and Vice—President for Pro- 33%,233 5,3 '
3 grams. He is a member of the American Society for Biochemistry and Molecular Biology. Professor Caprioli has been the 333;;
ii Editor-in-Chief of the Journal of Mass Spectrometry since 1990. He is currently co-editing a volume of Encyclopedia of ~¥§2 V
:3 Mass Spectrometry. In 2003, Dr. Caprioli received the Thomson Medal Award from the International Mass Spectrometry 3:43:33”
3 Society for "for outstanding achievements in mass spectrometry and for distinguished service to international mass spec- 3“»
33 trometry." 333513,,
,. mgr,“ 41331”:
E’ at John R. Yates, lll, Professor, Department of Cell Biology, Head, Proteomic Mass Spectrometry :‘Hség;
3 , ' a, Laboratory, The Scripps Research Institute. Dr. John Yates received the American Society for Mass 335+, “w
t, ' I Spectrometry research award, the Pehr Edman Award in Protein Chemistry, the American Society for 3E3,,3;‘s:;:_;,,;;
3i "' g . ' Mass Spectrometry Biemann Medal, the HUPO Distinguished Achievement Award in Proteomics, and .trygj'ég" 1;?!
33 3,3,, g. , , Herbert Sober Award from the ASBMB. He has published over 300 scientific articles. He received his ffiag $73155.
' 3 , first . j Ph.D. in Chemistry at the University of Virginia under Professor Donald Hunt. His graduate research 33‘??? 3., j}???
3 ,5? ._ ._ _,. - involved the development and application of tandem mass spectrometry for sequence analysis of pro- gflgzrfig,
3 " 1hr " teins. Following a Biotechnology Fellowship at the California Institute of Technology, he moved to the :52”
3 ,. ",3; Department of Molecular Biotechnology at the University of Washington where he attained the tenured 93:4,,
If t$12, , rank of Associate Professor. He is now a Professor in the Department of Cell Biology at The Scripps 3,3133%
33 Research Institute. His research interests include development of integrated methods for tandem mass fiaggmfif
'3, spectrometry analysis of protein mixtures, bioinformatics using mass spectrometry data, and proteomics. He is the lead M33» :3 5,;
3 inventor of the SEQUEST software for correlating tandem mass spectrometry data to sequences in the database. tfffii‘”
@3223 ”a
3 ‘ ml“ ; “.3 R. Graham Cooks, Henry B. Hass Distinguished Professor of Analytical Chemistry, Purdue 3%“,ggf
. g 33 University. BS, 1961, M.S., 1963, Ph.D., 1965, University of Natal (South Africa); Ph.D., 1967, Egg-1:
3 13;, 1', 3;, , , 3 Cambridge University; Fulbright Fellow, University of Warwick, 1981; Purdue Cancer Research ,5, ,
3i ‘ W 1' Lt:- ' ‘ Award, Indiana Lions Club, 1983; Analytical Division, Award in Chemical Instrumentation, 1984; 1‘,” {”31“,
33 ,_m_ ,, “‘57 E . Thomson Medal, International Mass Spectrometry Society, 1985; Sigma Xi Faculty Research Award, *9, ””431
3 31’31333’3 »_ 1986; Honorary Member of Chinese Mass Spectrometry Society, 1987; Herbert Newby McCoy 3,3Lfig,j,:
f3 ‘3‘253‘3313 23.33MB Award, 1990; Frank H. Field & Joe L. Franklin Award, (ACS Award for Mass Spectrometry), 1991; ,filu
3 "31’ Honorary Member, Ukrainian Chemical Society, 1995; Fisher Award (ACS Award for Analytical 31 ,w“. .
"‘ "1-3.- “ 25‘3”" *4"? Chemistry) , 1997; Outstanding Commercialization Award for Purdue University Faculty, 2005; Alex- 3331;433:135.
ander M. Cruickshank Lecturer, Gordon Research Conferences, 2005. Mass spectrometry is of in- @1333“;
. ' terest to this group, including fundamental phenomena, instrumentation and analytical applications. 3:33. 333*
' We study collisions of ions in the gas phase and at surfaces. The latter experiment aims at new Effigy;
methods of molecular surface analysis. In addition to reactive scattering, soft-landing of ions at surfaces has recently been ‘ -' ,I‘rgg‘E-g‘.
discovered. Development of the Paul ion trap and the construction of miniature ion trap arrays is the focus of an instru- “5: 5‘5;
mentation effort, the practical aims of which include in-situ on-Iine analysis. Ion motion simulations and laser tomography ,3 "
3 experiments facilitate the ion trap effort. We are currently employing ion/molecule reactions to recognize functional groups in 353$
'3 in polyfunctional compounds. Fundamental thermochemical properties such as proton affinities are being measured using 33,,”*°:{,¢
33 the kinetic method, which was developed from our earlier interest in ion structure and fragmentation mechanism. Our inter— 5; 35;~;33:=‘3,;=:.;;:;;-;
2 ests also include ion mobilities and other physical properties of biological molecules, trace environmental analysis and k‘vfig
3 atmospherically relevant ion/molecule reactions. Several new types of mass spectrometers have been constructed in Prof. ”A3”
Cooks' laboratory, including hybrid sector/quadrupole instruments and advanced ion trap instruments. Our group has yewg
r. made significant contributions to the development of desorption ionization and tandem mass spectrometry as methods of Wagggfig,
analysis of complex mixtures. "(55%;
:3 FREE PARKING is available at the William T. Young Library in the Visitor Parking Lot on Hilltop Avenue. Naff signs 35133339
5,] will indicate the reserved area. For additional information, call Professor Bert C. Lynn, Department of Chemistry, (859) fafni‘?
EI 257-2300 ext. 287 or by e-mail (bclynn2@uky.edu). 31*}? ’3', '
3 2006 Committee: Bert C. Lynn, Chair (Chemistry & Mass Spectrometry Facility), Boyd E. Haley (Chemistry), Mark A. Lovell (Chemistry) fig‘fi':
j 17,2333: figs; .1 ‘ j‘.
Symposium supported by the Anna S. Naff Endowment Fund .33, «$3,135.»
’ (additional support provided by the Office of the Vice President for Research, University of Kentucky) fig?