Networking event: Symposium on Biomolecular Structure, Dynamics and Function

Several of the more than 30 presentations and approximately 70 posters presented at this symposium, held at St. Jude Children’s Research Hospital on April 27-29, addressed the role of protein disorder in biological processes. Brian Volkman, Medical College of Wisconsin, described how the chemokine Lymphotactin performs different functions by accessing alternative native states that interconvert through excursions to the unfolded state. Shou-Ou Shan, CalTech, reported on studies of interactions between the signal recognition particle (SRP) and the SRP receptor (crucial to the control of protein targeting). She observed large conformational rearrangements that, by means of a disordered segment, allow part of the SRP receptor to alternatively interact with two distal sites on the SRP RNA. Ashok Deniz, Scripps, used single-molecule fluorescence techniques to characterize folding pathways for alpha-synuclein that may be relevant to Parkinson’s disease. Diana Mitrea, St. Jude, demonstrated that the nucleolar protein Npm’s functional equilibrium between unfolded/monomeric and folded/pentameric states is controlled by posttranslational modifications. Scott Showalter, Penn State, applied novel direct 13C detection NMR methods to the conformational and dynamic studies of FCP1 intrinsically disordered C terminus and its interaction with RAP74, a critical event in RNA transcription. Tanja Mittag, St. Jude, correlated her past studies of the dynamic interaction between the yeast ubiquitin ligase Cdc4 and its phosphorylated target Sic1 with new data suggesting that similar interactions may take place in human ubiquitination pathways. Other presentations, including those by the keynote speaker, Brenda Schulman, St. Jude, and Joel Tolman, Johns Hopkins, highlighted the importance of highly dynamic events in E1/E2/E3 ubiquitination cascades. A theme underlying several of Subgroups these quite diverse reports is the observation that disorder may be required to mediate functional mechanisms of many proteins that would generally be classified as ‘folded’. These new exciting results emphasize that ‘disorder’ can play roles even in the context of ‘order’, with fascinating and unpredictable mechanisms mediating excursions between these states.

The meeting was supported in part by a local networking mini-grant from the Biophysical Society.

Ariele Viacava Follis
   IDP Postdoctoral Representative

Membrane Biophysics

Call for Presentations:2013 Annual Symposium

The theme of the 2013 annual symposium will be Macromolecular Ion Channel / Transporter Assemblies. Subgroup members with exciting new data are encouraged to contact the subgroup chair, Diomedes Logothetis at, to express their interest in presenting at the symposium. Preference will be given to work that addresses structure and function relationships of macromolecular complexes. The program needs to be completed by the end of July in order to allow the Society enough time for appropriate exposure.


Bill Wimley named first Thomas E. Thompson Awardee

It is a wonderful illustration of Tom Thompson’s lasting legacy that the first recipient of the newly established Thomas E. Thompson Award for research excellence in membrane structure and assembly will be William C Wimley. He earned his PhD inTom’s laboratory at the University of Virginia by studying the biophysics of lipid-lipid interactions in multicomponent bilayers. Now a Professor at Tulane University, Wimley studies the fundamental structure-function relationships of membrane active peptides. Wimley will present his award lecture at the 2013 MSAS subgroup symposium in Philadelphia and receive a $1000 award sponsored by Avanti Polar Lipids, Inc. Congratulations, Bill. We are looking forward to your lecture!

Heiko Heerklotz, Acting Chair MSAS


July 2012 Table of Contents