Bulletin of the American Physical Society
APS March Meeting 2013
Volume 58, Number 1
Monday–Friday, March 18–22, 2013; Baltimore, Maryland
Session N43: Focus Session: Protein Misfolding and Aggregation III
11:15 AM–2:03 PM,
Wednesday, March 20, 2013
Hilton Baltimore Room: Holiday Ballroom 2
Sponsoring Units: DCP DBIO
Chair: Elsa Yan, Yale University
Abstract ID: BAPS.2013.MAR.N43.4
Abstract: N43.00004 : Amyloid Structure In Vitro and In Vivo*
11:51 AM–12:27 PM
Preview Abstract Abstract
(National Institutes of Health)
Solid state nuclear magnetic resonance (NMR) measurements can provide unique information about the structural properties of proteins in noncrystalline states that are of interest from both the biophysical and the biomedical perspectives. I will discuss recent results from my lab's efforts to characterize the molecular structures of amyloid fibrils, especially the A$\beta $ peptide fibrils that are associated with Alzheimer's disease. From a combination of solid state NMR and electron microscopy measurements, we have developed full structural models for 40-residue wild-type A$\beta $ fibrils that form in vitro and contain parallel $\beta $-sheets with 2-fold and 3-fold overall rotational symmetry. We have recently discovered that the ``Iowa mutant'' (D23N-A$\beta )$ peptide can also form metastable fibrils with a surprising antiparallel $\beta $-sheet structure. And we are in the process of investigating A$\beta $ fibril structures that develop in human brain tissue. In addition to recent results, I will briefly describe recent advances in methodology that contribute to this work.
*Supported by the Intramural Research Program of NIDDK/NIH.
To cite this abstract, use the following reference: http://meetings.aps.org/link/BAPS.2013.MAR.N43.4
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