xt74xg9f7d60 https://exploreuk.uky.edu/dips/xt74xg9f7d60/data/mets.xml University of Kentucky University of Kentucky Chemistry Department 19920413 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 Eighteenth Annual Symposium on Chemistry and Molecular Biology: "Protein Folding" text Eighteenth Annual Symposium on Chemistry and Molecular Biology: "Protein Folding" 1992 2017 true xt74xg9f7d60 section xt74xg9f7d60 —-——-——_~_————
Eighteenth Annual
———_—————______— ‘ . ‘ ‘ a ‘1‘", _
AM. PM. I .: l: .2 Symposmm on
9:00 Registration and Coffee—Room 137, 12:15 Buffet Lunch, Faculty Club (Please return ; 1. lil :- t;
Chemistry-Physics Building card by April 9, 1992 for reservations. Cost , > «g llfé l .
$7.00 to be paid at registration.) ‘ i . ‘5 ‘71 .
9:30 Welcome by Dr. Lee Magid, Vice President .I . i ,. If; ‘I emls
for Research and Graduate Studies, 1230 Dr. Kenneth Dill, University of California, .I‘ 5' ..
University of Kentucky, Room 139, San Francisco I:
Chemistry-Physics Building “The Stabilities and Kinetics of Protein
9:40 Introductory Remarks—Dr. Mark Meier,
University 0‘ Kentucky We are interested in the forces that determine the relationship
9:45 Dr. Robert L. Baldwin, Stanford University between the amino acid sequence of a protein and its structure M o lecular
“Pathways of Protein Folding" and kinetics, Usmg Simple models of short chains on lattices, we
search conformational and sequence spaces to find the relation-
There is general agreement today that structured folding ships between sequences and structures. We assume the domi» .
intermediates are populated in favorable conditions on the kinetic nant forces are hydrophobic interactions and conformational lo 0
pathways of folding of small proteins. A principal tool for entropies. We find that some sequences collapse in poor solvents
characterizing their structures is by pulse exchange with solvent to compact conformations with hydrophobic cores, secondary
(1H-2H) of the peptide NH protons in the polypeptide structure, and few native states (often only one). A significant frac—
backbone, followed by 2D 1H~NMR analysis after folding is tion of all possible sequences are relatively protein-like in water,
complete. Results of this technique show that native-like secon» i.e., compact and with much secondary structure. They fold along
dary structures, both a-helices and fi-sheets, are formed early in kinetic pathways, the cooperativity being due to conformational
folding. Equilibrium “molten globule" intermediates are attractive entropy. Interestingly we find that the problem of protein design .
subjects for study because it is possible to characterize in detail (Le. inverse folding: given a desired native structure, find a good
their structures and the interactions that determine these struc- sequence that folds to it) has much lower computational complexity ,
tures. Molten globule forms of different proteins exhibit a compact than the protein folding problem, which is computationally difficult.
conformation, a high content of apparent secondary structure, . - established in the memory Of
and few if any fixed tertiary interactions, Two classes of molten 2:40 Discusswn
globule forms are observed: structured molten globule in— . . Anna S Naff
termediates, with Liz-helices at the same location as in the fully fold» 250 D" 5351‘” van der Vies, DuPont Central
ed forms, and collapsed unfolded forms, which show no signifi- Research and Development . .
cant protection of any amide proton. Molecular Chaperones and their Role in _ "'—_ "-
Protein Folding" L0
1045 Discussion > 8 PROTEIN FOLDING
Molecular chaperones are defined as a family of unrelated classes 3:; O
10:50 Dr. Barry Honig, Columbia University of protein that mediate the correct assembly of other polypep» .59 ii (5 _———-————
“Hydrophobic and Electrostatic tides, but are not themselves components of the final functional g o 8
Contributions to Protein Stability” structures, The concept of molecular chaperones suggests that L E o SPEAKERS
_ _ interactions within and between polypeptides and other molecules U S V
The balance of forces that determine the denaturation free d b It d d h b b'l‘ ff . f “A X .
' f lobular roteins will be discussed Our ma'or con- nee to e contro e to re ucet e pro a my 0 ormation O O D‘ R b t L B 1d ‘
energies 0 g . p _ I _ ' . I) . incorrect structures. This control is exerted by pre-existing proteins “H :C 0 er ‘ a Wln
cluSions are: a) Ionizable amino aCids are slightly destabilizmg but . . . . . . . ‘H 0 ~
. I acting as chaperones to inhibit incorrect molecular interactions. C3 , Barry Honlg
make only a marginal contribution to the net free energy balance. . . . . .. Q) D\ C _
. _ _ . It is argued that in the assembly process there is a certain probability E 2:: 0 Kenneth Dill
b) The fact that the enthalpies of unfolding are quite small despite . . . . . a) +4
I l 'd f l b'l' . h l h t that incorrect interactions Will produce nonfunctional structures. 4: i... m S k Cl V ,
experimenta eVi‘Lence‘ 01a arge sta ”2mg ent .a py suggestst a Where this probability is small, self-assembly needs no assistance, ‘5 g) E as 1a van er les »
there must be a missing destabilizmg enthalpic contribution. c) . . . . Q. .._. x
h h d h b' ff . 't l d . 't d . t t but where it is high, molecular chaperones are essential to produce Q) c: Q)
t e y, rop 0 1C e ed '5 qu1 e arge an Its magni u e pom I5 0 sufficient correct structures for cellular needs. Q :3 ._.l
the eXistence of a large compensating free energy contribution. .
d) Both b and c can be explained by the cost associated with “bury~ 3150 Discussion Monday, April 13, 1992
ing" polar groups (including those that form hydrogen bonds) in Department Of Chemistry
the polar interior. Finally, our breakdown of free energy contribu- 4:00 Mixer. 0 University Of Kentucky
trons has led to the development of a relatively fast algorithm which _
distinguishes stable from unstable protein conformations. LQXIDQTOH, Kentucky 40506-0055
11:50 Discussion

 Eighteenth Symposium on
C h e mistry &
Molecular Biology
established in the memory of Anna S. Naff
Monday, April 13, 1992, 9:00 a.m.
Chemistry—Physics Building—Room 139
Department of Chemistry, University of Kentucky


Robert L. Baldwin, D. Phil, Oxford Univer— Barry Honig, Ph.D., Weizmann Institute of
sity, England, Rhodes Scholar. Postdoctoral Science, Rehovot, Israel. Postdoctoral Fellow,
Fellow, University of Wisconsin, Guggenheim Harvard University. Professor, Columbia
fellow, Copenhagen, 1958. Visiting Professor, University, Department of Biochemistry and
College de France, Paris, 1972. Professor of Molecular Biophysics. Associate Editor, Jour—
Biochemistry, Stanford University. National nal of Molecular Biology. Editorial Boards:
Academy of Sciences, American Academy of Biochemistry; Proteins. President, Biophysical
Arts and Sciences. Stein and Moore Award of Society, (1990-1991). Topic: “Hydrophobic and
the Protein Society 1992. Editorial Boards: Electrostatic Contributions to Protein Stability.”
Proteins; Biochemistry; Protein Science; Bio-
polymers. Topic: “Pathways of Protein Folding.”

Kenneth Dill, Ph.D., University of Califor- Saskia van der Vies, Research Assistant,
nia, San Diego. Postdoctoral fellow, Stanford Agricultural University, Wageningen, The
University. Professor, University of California, Netherlands. Visiting Research Assistant, Plant
San Francisco. Adjunct Professor, University of Breeding Institute, Cambridge, England. Ph.D.,
Utah. Editorial Boards: Biopolymers, Protein University of Warwick, England. Research
Science, Biophysical Journal, Biophysical Fellow, University of Warwick, England.
Chemistry, Protein Engineering. Topic: “The Postdoctoral Visiting Scientist, E. I. du Pont de
Stabilities and Kinetics of Protein Folding.” Nemours, Wilmington, Delaware. Topic:

“Molecular Chaperones and their Role in Pro-
tein Folding.”
Parking available free at Commonwealth Stadium on Cooper Drive. Shuttle buses run to the main campus. Additional parking '
(for a fee) available in UK Medical Plaza Parking Garage, located approximately one block south of the Chemistry-Physics
Building; this garage can be accessed from both Rose and Limestone Streets—look for Medical Plaza Parking signs. For addi-
tional information, call Mark Meier, Department of Chemistry, (606) 257-3837.
Symposium supported by the Anna S. Naff Endowment Fund.