North Jersey Section
American Chemical Society

Jan 22, 2014 – NMR Topical Group Meeting

The North Jersey ACS NMR Topical Group proudly presents its January monthly meeting at Rutgers CABM on Wednesday, January 22, 2014[ register ]

VENUE: Our meetings this year are at the CABM (Center for Advanced Biotechnology and Medicine) on the Rutgers Busch Campus, 679 Hoes Lane West, Piscataway NJ 08854 [ map & directions ].

The meeting is in Room 010, which is located near the main entrance of CABM. Parking is available in the lot across the street from the CABM building. Dinner will be served in the meeting room.

Featured Speaker

“Unraveling the Structural Organization of Amyloid with DNP-enhanced MAS NMR Spectroscopy”

Galia Debelouchina, Ph. D.

Princeton University, Princeton, NJ

Program

6:00 pm  Dinner

7:00 pm  Seminar

Meeting Venue

CABM (Center for Advanced Biotechnology and Medicine) on the Rutgers Busch Campus

      679 Hoes Lane West, Piscataway NJ 08854

Dinner cost: $15 (no charge for students / postdoc / retired / unemployed).

No charge for seminar only.

Extra Door Prizes!

(2 door prizes for # of attendees < 20, 3 door prizes for # of attendees > 20)

Register: Online below or via e-mail to Swapna Gurla at gvts@cabm.rutgers.edu.

Abstract:

Amyloid fibrils are insoluble, non-crystalline protein filaments associated with a number of diseases such as Alzheimer’s and Type II diabetes. They can have a functional role in different organisms, and many proteins and peptides have been found to form amyloid fibrils in vitro. This talk will present an overview of what is known regarding their molecular structure, focusing in particular on the fibrils formed by an 11-residue segment from the disease-related protein transthyretin (TTR). This system exemplifies our efforts to characterize the hierarchy of structures present in the fibril form, including the organization of the β-strands into β-sheets (tertiary structure), the β-sheet interface that defines each protofilament (quaternary structure), and the protofilament-to-protofilament contacts that lead to the formation of the complete fibril. Our efforts resulted in the measurement of 110 distance and torsion angle constraints (10 per residue) across all levels of structural organization, resulting in the best resolved amyloid fibril structure so far. The structural investigation benefited extensively from the development of dynamic nuclear polarization, a method used to enhance the sensitivity of MAS NMR experiments, and leading to unprecedented gains in signal-to-noise ratios and acquisition times.

(2 door prizes for # of attendees < 20, 3 door prizes for # of attendees > 20)

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