North Jersey Section
American Chemical Society

Feb 19, 2014 – NMR Topical Group Meeting

The North Jersey ACS NMR Topical Group proudly presents its February monthly meeting at Rutgers CABM on Wednesday, February 19, 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

“Mapping Protein Folding Landscapes Using High Pressure NMR”

Catherine Royer

Department of Biological Sciences
Rensselaer Polytechnic Institute


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 employed/ $5 for students, postdocs, retired and unemployed

No charge for seminar only.

Register: Online below or via e-mail to Swapna Gurla at


Despite significant progress in recent years in understanding protein structural dynamics we still lack sufficient experimental knowledge of protein folding energy landscapes. Moreover, we cannot predict folding transitions states or routes from amino acid sequence or structure. Nor is it known how sequence encodes the conformational fluctuations and heterogeneity required for protein function in specific contexts. We have recently demonstrated that pressure induced unfolding occurs largely because of specific packing defects or void volumes, in the folded structures of proteins that disappear upon unfolding, leading to a decrease in molar volume. Unlike denaturant or temperature perturbations, the effects of which depend on the amount of exposed surface area in the unfolded states of proteins, pressure effects depend on specific properties of folded states. And because packing defects are local and specific, pressure perturbation acts locally to decrease volume, thus allowing for the characterization of intrinsic folding cooperativity. Pressure also provides access to conformational states inaccessible by other methods. Coupling high pressure with multi-dimensional NMR is particularly powerful, as it provides site specific observables throughout the structure of the protein. Used in steady-state and p-jump mode, high pressure NMR has revealed unexpected complexity in the folding rates and routes of cavity-bearing variants of Staphylococcal nuclease. The results underscore the subtlety of the sequence determinants of folding landscapes.