Subgroups

Membrane Biophysics

Greetings, MBS members. Our Annual Membrane Biophysics Subgroup Symposium will be held on February 25, 2012. The theme for the 2012 Symposium, organized by the Subgroup Chair, Paul Slesinger, The Salk Institute, will be Dancing with New Structures: Insights into Transport Function. Scheduled speakers include Jeff Abramson, UCLA; Wayne Hendrickson; HHMI/Columbia University; Pierre-Jean Corringer, Institut Pasteur; Christine Ziegler, Max Plank Institute of Biophysics; Bill Catterall, University of Washington; Youxing Jiang, HHMI/University of Texas Southwestern; and Slesinger himself. The detailed program is listed on the Subgroup website, http://www.biophysics.org/MembershipSubgroups/Subgroups/MembraneBiophysics/tabid/513/Default.aspx.

The symposium will be followed by the annual Kenneth S. Cole Award Dinner, which will be held at the San Diego Wine and Culinary Center (additional details forthcoming). Be sure to attend the symposium and dinner to hear the latest about transporter and channel structure and function and socialize with fellow biophysicists!

Jackson Named 2012 Kenneth S. Cole Awardee

There were a number of outstanding nominations for the annual Cole Award, presented to a scientist who has made significant contributions to our understanding of membrane biophysics. After careful consideration, Meyer B. Jackson, Cole Professor of Physiology at the University of Wisconsin (yes, that Cole!), has been selected the 2012 Kenneth S. Cole Award winner. Jackson is recognized for his seminal work on ligand-gated receptors and on the biophysical analysis of synaptic transmission, most recently focusing on synaptic vesicle fusion. Jackson will
receive his award at the subgroup dinner following the annual symposium.

Subgroup Email List

The Membrane Biophysics subgroup has an email distribution list. Members may contact Mike White (mwhite@drexelmed.edu) for information
about sending out email announcements of conferences or meetings.

Mike White, Secretary/Treasurer

IDP

Call for Submissions for IDP Postdoctoral Research Awards

Two awardees will each receive a $500 honorarium and present a short talk at the IDP Subgroup Symposium on Saturday, February 25, 2012, in San Diego. To apply, submit an abstract for a poster to be presented at the Biophysical Society Annual Meeting. Select “Intrinsically Disordered Proteins” as a topic area (this can be submitted as a “Late Abstract”).

Send the abstract, along with its BPS abstract control number, via email directly to the IDP Subgroup at IDPsubgroup@gmail.com by December 15, 2011.

Instruct your advisor to email the Subgroup at IDPsubgroup@gmail.com by December 15, 2011, confirming the postdoctoral status of the applicant. Only those who are postdoctoral scholars/fellows at the time of abstract submission are eligible for an award. The selection committee will choose the top two abstracts from those submitted on the basis of scientif c quality and diversity with respect to the topics to be discussed by the other invited speakers. Please address all inquiries to IDPsubgroup@gmail.com.

IDP Pedagogy, Part III

This article is the third in a series of articles illustrating how IDPs are taught across the discipline. Look for subsequent installments, as well as a continuation of this article, in future Newsletters.

In the first installment of this interview, which appeared in the October 2011 issue of the BPS Newsletter Richard Kriwacki, St. Jude Children’s
Research Hospital, explained how he introduces IDP structure-function relationships through emphasizing their significant biological roles. In this final installment of the interview, Ryan Hoffman, IDP Subgroup Postdoctoral Representative, probes the theoretical motivations for Kriwacki’s approaches.

Do you present IDPs as part of a continuum of order, or as discrete states?

I’ve been a proponent of the continuum perspective since I fi rst started talking about IDPs. I’ve always acknowledged that proteins can exist in many states of order and disorder. I would use my early work on p21 as an example of a protein that is pretty far to one [disordered] end, but not all-the-way to one end, as these kinase inhibitors exhibit partially populated structure in isolation. I’ve always used enzymes as examples toward the [ordered] end of the continuum, but not all the way at the other end, as dynamic fluctuations are critical for catalysis.

And the point I always make is [that] we’ve had relatively little awareness of the disordered end of the continuum. And I often will say to an audience, ‘It’s hard to study disorder. You need to use techniques that are diff erent from what’s considered mainstream structural biology techniques. It’s hard work to establish relationships between disorder and function.’ Five or ten years ago there wasn’t a lot known about these relationships. We had to invent the approaches and even the paradigms. It’s taken a while to understand the disordered end of the dynamic continuum but significant progress is being made, and I hold hope for the textbooks someday having in the early introductory chapters information about how biomolecules work, how they perform their functions, and some illustration of this continuum. This could serve to organize later sections. I guess that may occur in the future.

When I think about protein-mediated mechanisms or any kind of biological mechanism at all, there’s always some amount of dynamics in the picture...

It’s almost implicit.

...thinking of things as static functional units doesn’t come from an understanding of mechanics or macroscopic machines, so why is the involvement of conformational fluctuation in protein mechanisms seen as exotic?

There’s this historical bias in the structural biology field from crystallography that sort of set the stage for the existence of this obstacle. This is not a criticism; crystallography emerged in the ‘60s and has been a primary tool, and continues to be a dominant tool in understanding what proteins look like. I think the early days of structural biology were dominated by that approach where you have elegant three-dimensional pictures of proteins from crystallography, often times coupled with very deep probing of structure function relationships through mutagenesis and functional assays. Th e textbooks are just full of information from that perspective and students get introduced to this when they first get introduced to biochemistry, which is currently in high school. So this sets up the perspective that this is how you view proteins. And DNA is represented as being static as well, and of course there are all sorts of dynamics required for the processes that DNA participates in.

And it’s hard to represent dynamics.

You need movies. Or you need lots of static frames stitched together with good annotations to imply motions. Representing dynamics is hard, but in the last ten years there’s certainly been good scientific progress in understanding how dynamics are critical for biological processes, ranging from enzyme catalysis to dyneins that transport cargo, everything in-between, the nuclear pore complex, signaling mechanisms. So I think more and more students are being introduced to the importance of dynamics.

Jianhan Chen, IDP Secretary/Treasurer


November 2011 Table of Contents