xt7h9w090702 https://nyx.uky.edu/dips/xt7h9w090702/data/mets.xml University of Kentucky University of Kentucky Chemistry Department 20000407 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 Twenty-Sixth Annual Symposium on Chemistry and Molecular Biology: "NMR Spectroscopy in Biological Chemistry" text Twenty-Sixth Annual Symposium on Chemistry and Molecular Biology: "NMR Spectroscopy in Biological Chemistry" 2000 2017 true xt7h9w090702 section xt7h9w090702 9.6171354“ 9555 ,ggIrgcfiz. ,- . $2 _.~‘ 9%?‘:"='-. 4'4,:“:I.,; 3:.zrxsctr-iics.,9.-:- '-‘-9:-,- :3: . :»:-v:~:a .2: r ~~.:,<..r.«g:. : 4 mm 7» w, - .:.- , ,. -~ 4 :9 » .. . » » - 4 ~ ~ -- 4
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2000 PROGRAM $33,394} Twenty-Sixth Annual 1
8:30 am. Registration and Continental Breakfast of addition in fullerene derivatives Th ‘ :43???» S m OSium on l
. . . . us, we ar v i ‘ 4X ‘« '- 1"" --
Atrium (Room 1-65), William T. Young Library of fullerene reactivity. e de e oping a theory " . 2:). ll" y p 't-‘E 3’?
. 2. . 9-4::- .~ :I-i“ .: «. 33;,
9:00 a.m. Welcome by Dr. Fitzgerald Bramwell Vice . . " 25'!7,‘,“-::-:1-:lé:i ' f3" --
ls... Chemistry
. . _ . . _ . . , . s ~2: . ._ "’3’" 9 4 - 33,341; 3,-2.5.
lLI’Vrillll‘ilerhSITygulfizntllggry Auditorium (Room 1 62), g, hellfifo'" aId‘gnce or at regis‘rafion: Faculty/ gig-mi. .9191}? 9.; 2’1"»: fps:
- ues .00; raduate Student ($5.00).] 16'4"" »r l" & 2455'"
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Sniegrus‘ittycl’rgf $3an2; Dr. Anne-Frances Miller, . 2.00 pm. Br. Stanley J. Opella, Universny of Pennsylvania ll?" :45: ‘52:“ ”1:?
9 10 D . NMH Spectroscopy and Functional Genomics" ;.3,::’ Q hi": "I: M o I ec u lar $31 slitlll' ‘3’:
a m agIallIiIcgiraeeégufiiiirmers, Universdy of Maryland IITheI striiictures of indiwdual proteins and their complexes with “flit“? l at}, 7"»;
i: . _ . . sm.a mo ocu es, peptides, and nucleotides are being determined at .l 5 ' "l; 5’
nggvfiglsdlzgsglmxl Genome ”9509mm” 3’7" an increaISIngly rapid rate. However, most biological functions are car- 91%- {-25:5392. BlOlogy 9, l :l'
ried out in a coordinated fashion by groups of proteins from a single 4429,4132" "-9! 2‘2}: "ll-r3193 “'9
Progress made toward understanding the molecular determinants operon or large complexes organized as supramolecular structures, lfit’lfiéfilrgll' fll‘r‘“
of HIV-1 genome recognition and packaging will be presented. Cur- such as membranes 0' Viruses. A5 a "35“”: mo structures Ol only a l" 2'" "4 '3‘" 'le‘:‘£l$:p”fll‘lfi
rent studies focus on interactions between the HIV-1 nucleocapsid fraction of the proteins can be solved using currently available high l gig. 339;:Yw5
Protein and the stem loop recognition elements of the Psi-packaging throughput melhOdS. OHlY In exceedingly rare cases Will all the struc- * ill-lit: Elli—"I‘Hél-qzfifi
signal. including RNA stem loops SL2 and SL3. In addition, structural Mal and regulatory proteins Of an Ioperon 0" virus crystallize l” forms ' lll'llfeiflyn- {3, 'fiéffi 1
studies of the capsid proteins of the HIV-1 HTLV-I and RSV retroviruses swtable for x-ray diffraction or reorient rapidly in solution for NMR ap- 'zi~3“.5€7=‘~"ifel‘"."l‘ 3,.4'5-5.;;.£«.I._§; 9‘
suggest a new mechanism for capsid assembly that involves oxida- proaches. Further, proteins in complexes typically aren't Soluble or, if “-41:51?“ %‘ fig“; 3“?
tion of conserved cysteines, triggered as the assembly virus enters they are soluble, don’t reorient rapidly in aqueous solution. Fortunately, 75$???» "W
the oxidizing environment of the bloodstream. solution NMR methodspan be adapted and solid-state NMR methods 21:" .l if~".'.:7=‘~"":+. l‘i’vfifil‘wi‘ifi"
are well suited for studies of slowly reorienting, immobile or insoluble 15": =i~2~liléhlzlv"
10:10 am. Break molecules. Examples of how NMR can be used to characterize the 9 9):".‘5. i 35" s" " l ‘22"!
. . . . . . structures and dynamics of many proteins found, or soon to be discov- ‘l7:-""~";““f ll N l " 5,23“. l a ll“ 3
10.30 am. [5:33:97 E. Wemmer, UmvefSIlY of California at ered, in the course of sequencing genomes will be discussed. 113“} l“: «993$
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"A Structure Based Approach to Design of 3:00 pm. Break i;‘.‘”-§'T.-".T*~j7‘;x-:f established in the memory of gizfligéigifi
Sequence Specific Minor Groove Ligands" 3:20 pm. Dr. Ad Bax, National Institutes of Health £3255“ Anna S Naff )figz-tfig,
:: . . 4 .. ' .ii'. :lfi?" ‘ "-.
d Some years ago we began stmctural studies of the natural prod- PygIcelIIeIaerIIl/Iagnetic Resonance Of Weakly Aligned frag; 1?; 3:3}? 52;):
uct istamycin-A, which binds to A-T rich sequences in DNA using Q" j “if”: 2 WV
. I . . . I I I . . ;. :_. +4.3'1'G'fl —— .v" .. :.‘-.-:—"»*
2,94}; SPeClIlI'IOSCOPY- With a minimum binding Site of four consecutive d' l WIetIak alignment of molecules results in incomplete averaging of .l;«.1§::.nj:¢.‘cggs '.‘.1":“§*€
' Pairs t e distamycin bound in the center of a re ion of narrow 'Po 3“” eractions. Provided the alignment l5 extremel weak "103: ll" illfifllfllill 2‘ I r: if};
minoigroove- As we looked at other combinations 0% A-T pairs we tIheINMR spectrum retains the simplicity and high resolution of (regular iii-:95: 3] NMR speCfroscoRy In '1‘;$,‘{+
identified a new lYPe of complex. one in which two distamycin mol- “(two state NMR Spoctra, but nevertheless permits measurement of In {2" BIOIOQICOI ChemIS” Y 'f:':‘.‘;:§‘.1‘:5 i-ifi'
eCtiles bound Side-by-side and antiparallel, in a region of wider groove. one- and two-bond dipolar interactions. These provide information 0” 8 {kl/:2“? ‘ "'5" ———-——-——— :3” ‘2
This slfuotureIleed us to consider groove width as a major factor in the orientation 0' internuclear vectors, Wthh complements the con- b O '5“? 3;»? ll; 3:23:12;
d.Gtermining binding affinity. and allowed the successful implementa- ventional NOE and J coupling parameters. SUCh measurements ”Ol 7’3 >‘ \t'D Kill-"iii" l '3‘.f',;=,;:l,'§7;i‘f
"on ofI a hydrogen-bond based recognition of (3-6 base pairs. To only make structure determination more robust, they also promise to E % o "wmgcév'5i hi“: 3,.
maintain high sequence specificity, and to enhance affinity, it was Iogi- expedite the process and to extend the size Of proteins whose struc- a.) 5 ‘0 lb!” 2 1:2: SPEAKERS (ad; :2”:
cal to tether the ligands together. With a combination of these ideas it - ture can be studied by NMR .1: E 8 l ‘ :55'2’1-‘21‘552'2 Ad Bax W'fi
is now possible to design a ligand to bind almost any DNA sequence . - - - U a.) [2'2"irl“ llzllf‘ll' 57,5465155
of interest with high affinity (dissociation constants in the nanomolar 4'20 p.m. 323Tg§333§§£§'5292’,"§§'?;3¥n°,§;§,§"§"°k¥ “-l M >" 2" +" by? Stanley J- Opella I: jgx‘tyl";
range) and good specificity (incorrect sequences being bound 10-100 copyq' y pec ros- o “l“ M a“; “fit," 2 ' '1‘: f;§;-."‘.;}'i$if’;k?~
fold less tightly than correct ones). The evolution of this design, and E o o 3393:1235 MIChael F' Summers )‘mih’d
the cgrrentIstatIe of our understanding of the binding modes will be I Essentially all of the chemical reactions in our bodies, and in ‘1) 3" g +x‘é‘4t‘l David E Wemme fiEgllglxlla:
described in this talk. Examples of the uses of such ligands in a biologY. are mediated by enzymes which catalyze and control each E '5 ._. Egéifit‘T-‘iiélir2: ' r y“:
biological context w." also be given. reaction. Most of the reactions involved in respiration and primary 3% B 2:0 l5¢§‘~%re “toxic "'5
. metabolism involve gain or loss of electrons and are thus “redox” reac— ‘1‘ ,2, "—9 ‘f‘ ‘fi'fivk - - 13%“;
11:30 am. Br. H. Peter Spielmann, University of Kentucky tions. We 3"? ”5mg NMR SPGCll'OSCOPY to learn how relatively large, 0 ‘3 SE lit-555333 Elli-"713;". FI'IdGY, Apr” 7’ 2000 33 {2‘ 15.1‘1
NMFl Spectroscopy of Novel Materials” Slfow and fleXIble molecules such as proteins can control the activities O D 9—] 35“" l; 1; '2 r": l‘ls‘l‘lfl";
0 individual tin , fast, delocalized electrons, for such cont ' ' N'T‘V‘ifilw' ”All? ’3’ 93"“
I FullerenIes are a new allotrope of carbon with new uses, proper- to life. y rol Is cru0ial “(*“e;4.; D rt f Ch ' it} 51;"
ties and pOSSIny, new synthetic rules. Therefore, we are using 13C . :;I;§;~;g:.I’1-i:;é;}§rg epa ment 0 emIStry 21*“
NMR spectroscopy and theoretical calculations to correlate chemical 5:00 pm. Optional Tour °f the New NMR Facilities ”le ‘5 l: Unive It f K t k I} Villlfi‘ 5:22.,
. . . I . . . . I . i g l'Sl y 0 en uc y ma.
shifts, pyramidalization, and hybridization With observed regiochemistry - 2' ages“, ' 3:24.909, ‘
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Department of Chemistry, UniverSIty of Kentucky a“,
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NMR Spectroscopy in Biological Chemistry
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1:; Ad Bax, Chief of Section on Biophy51calNMR Spectros- Stanley J. Opella, Professor of Chemistry, Umversrty of C “frigate
copy, National Institutes of Health. Ph.D., Delft Univer- Pennsylvania. Ph.D., Stanford University; Postdoctoral ~£i§
3Q sity of Technology; Allan C. Davis Medal of the Maryland Fellow, Muscular Dystrophy Association of America; Alfred Mg'
'3 Academy of Sciences as Maryland’s Outstanding Young P. Sloan Research Fellow; Adjunct Professor, Wistar Insti- its,
Scientist for 1987; NIH Directors Award; Gold Medal of tute; Bernard E. and Ida L. Grossman Professor, Member, Ffisgflf-f ..

the Royal Dutch Chemical Society; Bijvoet Medal of the Biophysics Panel, National Science Foundation; Member, ‘ffigg‘i
Bijvoet Center for Biomolecular Research, Utrecht Univer- BBCB Study Section, National Institutes of Health; Editor, fl $313 5
sity; The NIH Lecture Award; The Young Investigator Award Journal of Magnetic Resonance. F543;? §4§§i
of the Protein Society; Correspondent Member, Royal Neth— '3 3'; "£33251

. erlands Academy of Sciences; EAS Award in Magnetic Reso- gfitfr; :7

: nance; Hillebrand Award of American Chemical Society; E. L,v§;.§~§a.‘:
7;: Bright Wilson Award of the American Chemical Society. Egfifi
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, Michael F. Summers, Professor of Chemistry & Biochem- David E. Wemmer, Professor of Chemistry, University iK , 3‘31 7-";
ii istry and Howard Hughes Medical Institute Full Im'cs- cf Califcrnia at Berkeley. Ph.D., University of California €59rf‘
‘a tigator, University of Maryland Baltimore County. Ph.D., at Berkeley; Postdoctoral Fellow, Universitat Dortmund; if" 3:?
g Emory University; University of West Florida Distinguished Operations Manager NIH NMR Facility, Stanford Univer- “lgilgifipghgu
it Alumnus Award; Member, NIH Reviewers Reserve; Chair, sity; Member Sigma Xi, Berkeley; H. C. Brown Lecturer, M‘sfif’f’:
Advisory Council, National Magnetic Resonance Facility Purdue University; Miller Research Professor, University ”3me
at Madison; Member, NIH Study Section BBCA; Editor, of California at Berkeley;Editor, Biopolymers Nucleic Acid a; f3”
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- 2 Board of Protein Science; Maryland Distinguished Young fawifif:
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i; Investigator Award; NIH Merrit Award; Eastern Analytical 55:" 1“???

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tem of Maryland Regents Award for Excellence in Research. if; 3135‘:

j‘ Free parking available at the William T. Young Library in the Visitor Parking Lot on Hilltop Avenue. Additional parking (for a liegfi f .3; fr?

fee) available in UK Medical Plaza Parking Garage, located approximately one block south of the Chemistry-Physics Building; Efé E; :5:

, this garage can be accessed from both Rose and Limestone Streets - look for Medical Plaza Parking signs. For additional informa- fig? 1;} f’

‘3 tion, call Professor Anne-Frances Miller, Department of Chemistry, (606) 257-9349 or by e-mail (afm@pop.ul§ér

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Symposmm supported by the Anna S. Naff Endowment Fund £355; 'th

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