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2009 PROGRAM 5.,._.,,g ThirtyFifth Annual ;: 1
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_____ .2 s ~ Symposmm on .
8:30 am. Registration & Continental Breakfast, tively, assembling into structures containing parallel 3 a) :5. . " :21..
Room 137 Chemist -Ph ' B 'Id' d  II I h r ' ' -h I' I I t - C  C 0. .
, ry ysrcs ur mg an anti para e eices, extensrve inter eica eecro as) a 2 0 . . ,1. . . , .'e"--:;' . ;
static interactions, and a solvent-excluded hydrophobic 5 8 - _Z r.-.-. 1,5 , Chem Istry  1?? 553.3% 11","):
9'00 a.m. 33339 axigrr'sr"LtflieRtSUEbasAamy core. Ongoing efforts to elaborate beta-peptide bun E 3'). :3 E E tr .... 1'2}
139 Chemist -Phtysics BuiIst: y 00'" dles with enzyme-like metal-binding and catalysis sites DE: 3' gig:  gig." & : :L'L.:_,,.j.-.7 2';
. Y Y 9 will also be described. e a , J - .. ..ri'itfii
9:10 am. Introductory Remarks - Dr. Steven W. _ 2 _' L; M I I LY
Yates, Chairman, Department of Chemis- 12:00 pm- Poster Sesswn. Rose S_treet Concourse, :55; .148: . -. O ecu ar :gf_.:jja};ln
try, University of Kentucky Chemistry-PhySIcs Budding ".I..;' " '-:-r'. _ ' _ an? '35,}
. . . . diam; B I "- ii" L'
9:20 a.m. Dr. Michael H. Hecht, Princeton UniverSIty lunch. Conferen_ce_Room (GP-137). Chem- ,5: IO 09y _.
"Towards Synthetic Biology: Functional IStFY'PhYSICS BUIIde . #1,: ' < -'.-,;' ff"
De Novo Proteins From a Designed Artifi- _ . 3 J .
ciaIProteome" 1.30 pm. Dr. 'Peter G. Schultz, Scripps Research 3 it 93. \ 1,
Institute  ' ,1, ' . g "'-::; "._ [355
. . . . " ' '  l " 15 ii
Synthetic biology aims to desrgn and construct agncgfgyt [Encemlnsteggcgezg ghffggg  '99. mi / /' '3';.~...-r.I...'_-.".f*i
biological systems from dened components. Initial en-C Code". .39"; 7:91.: 3/ V 1?
efforts in this eld typically rely on toolkits of genes . , / , . 43.3 '
and proteins borrowed from preexisting organisms, Our research program combines the tools and  l . V
and recombined into novel arrangements. In contrast, a - . ~ - " :1 ~. Life;
truly synthetic biology would incorporate novel macro- p rinCIples .O-f chemistry with the molecules and proc 759.,1'1 1: 4...}?
molecules designed from scratch and synthesized in esses Of V'ng cells to synthesrze new 'TO'eCU'eS and '53. i 13 3}?
the laboratory. As an initial step toward this goal, we modletcullar .aSISSmblies Wlth novel. physrcal, chemical ,.1 established by M Benton Naff ~
have constructed a collection of de novo roteins (an an IQ ogica unctions. By studying the structure and by, . - .
articial . roteome) com risin millions 8f desi ned function of the resulting molecules, new insights can be "535? In memory 0f Anna 3- Naff E :lftegw
roteins PI'his resentatian will9 demonstrate that9 ro- gained into the mechanisms 0f complex biological and 1%? a"? 34.
p. ' . p . . . p chemical systems. Examples of this synergistic chemi- $49.29., ,.-'i.1?:r";;3.:tifsiiz
terns from this articral proteome fold into well-ordered . - - - - '- t 2'  . at
structures and e rform a ran e of biochemical and bio- cal/biological approach to synthesrs Will be discussed ~ .3; V._'._-j,,,;3.f' . . 5.3.7.35" agar}
Io ical function: 9 including the addition of amino acids with novel biologi ijrQ'..o' " V Pratem Desrgn and { {if-
9 ' cal, chemical and physical properties to the genetic L0 . )7 En9meenn9 3
_ codes of prokaryotic and eukaryotic organisms, and the >, L0 '5}, " . 1' ~* ,r"5
10-30 3-m- Break (Refreshments AV3"ab'e) identication of small molecules that control stem cell *3 >8 iii: .,, 2.1%.}:
. . . . $731.9:- . #1., W44. ,,,~v,
10:50 am. Dr. Alanna Schepartz, Yale University self-renewal. and directed differentiation, as well as E 5 (5 H. . SPEAKERS ..;;'.'.:.;.-5
"Protein Design Without aAmino Acids" reprogramming 0f somatic 395- g 3 8 f 'T'J C 1&32,
4: O -- ..ij '2.,_ t Fig}? .113: 1.3;-
- - - ' - - O C  3-:  . I
The catalytic, mechanical and structural tness of 2-40 p.m. CIOS'"9 Remarks ' Dr._ "9!" we" Depart- ... 2 : 1 4' Michael H. Hecht iv~
proteins rely on their ability to fold into discrete secon- ment 0f Chemistry, UniverSIty 0f KentUCky g u x a; 7., Alanna Schepartz f if
dary, tertiary and quaternary structures. Non-natural g i  Err. P t G S h It 11'7?
polymers have the potential for equally complex struc E r: S g 9 er - C u Z r4563;
ture and sophisticated function, but the design of such 1: g *5) 25,9; 2.1;
molecules is even more challenging than protein de 5 > C 53 . . *
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Sign, because there exrst no natural templates to a) C E Rf: Ha Frlday April 24 2009 atmqr
mimic. This lecture will describe the design, synthesis, 0 D ' 3:255? 1i. %.L,
highresolution structure, and biophysical analysis of a I 1;. . 35:33 131?:
series of helical bundle proteins composed entirely of {it"fgi;_~__11f{_'.{'~7?fi:1}-j"' Department Of Chem'Stry "131
betaamino acids. Like natural proteins containing al~ _ O f  University Of Kentucky watgut
phaamino acrds, betapeptide bundles fold coopera ihtth/wwwchemukyedu/semmars/nal) 75:359.;- Lexington, KY 40506-0055 as
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