Report on a trip to 2004 FASEB Summer Research
“ Protein Misfolding, Amyloid and Conformational Diseases”
Destination: Snowmass Village Conference Center, Colorado, USA
Purpose of the trip
I have been studying the fiber structures formed by yeast prion Sup35.
The purpose of this trip was to present our recent results and discuss
with many people at the meeting to think about the direction of our
future research. I also wanted to learn more about protein folding
including those in amyloid fibrils and explore the world wide research
trend in these fields.
Schedule of the trip
6/11 ITAMI (Japan)→NARITA (Japan)→SAN FRANCISCO (USA)→DENVER (USA)→ASPEN
6/12-17 2004 FASEB Summer Reseach Conferences
6/18-19 ASPEN (USA)→DENVER (USA)→SAN FRANCISCO (USA)→NARITA(Japan)→HANEDA(Japan)→KANSAI
This Conference was a definitive meet for researchers studying amyloid.
I presented a poster on the structural analysis of yeast prion Sup35
fibers. The main point of my poster presentation was that our fiber
diffraction strongly suggests that the structures of amyloid fibers
formed by Sup35 fragments are ß-helix, not a stack of ß-sheets as many
other groups in the field have reported to date. Ronald Wetzel (Tennessee
Univ.) studied the proline mutants of Aß(1-40) and suggested
that the core structure of Aß(1-40) fibers is not a stack of ß-sheets
triangle form. The group of Robert Tycko (National Institutes of Health)
reported interesting data, too. Aß(1-40) fibers formed in agitated
or non-move condition showed differences in structural features. Agitated
and non-move fibers were observed by TEM, and the differences in the
appearance between these two types of fibers seemed to be the number
of protofilaments, periodicity and so on. These fibers labeled with
13C were analyzed by NMR, and the 13C-13C distances were measured,
and the distance between some residues was different in two mutants.
Thus, different fiber structures formed under different physical conditions.
Perspective and future plans
Helen R. Saibil (Birkbeck College London) and Louise C. Serpell (Cambridge
Univ.) observed long periodicities of fibril structures and showed
that they are variable by using electron microscopy. But, the structure
of the fibers were different under different physical or solution conditions.
We have to analyze the fibers formed under various conditions, and
collect more solid structural proofs that the core structure of the
fiber is ß-helix.