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Transition 2006: Seth Robia has finished his postdoc stage in Thomas Lab and moved not too far away, at Loyola University in Chicago, IL, as Assistant Professor of Physiology. Two of our Junior Scis, Kari Pedersen and Cory Paterson have been accepted into Pharma and Med Schools, so good luck to them. [July 06]
Transition 2005: Our collaborator Ed Balog moved out for a tenured position at Georgia Tech. Cheryl Miller has also left the lab, after 16 years, to prepare business models for an emerging private enterprise. [July 05]
This year Dr. Thomas was elected chair of the Gordon Muscle Conference,
to be held in the summer of 2011, at Colby Sawyer College in New Hampshire. He
has also been invited throughout the year to give talks at conferences and
symposia such as The 11th
International ATPase Conference at Woods Hole, MA in September,
The Gordon Conference on
Muscle Proteins, in NH in July, and invited talks at major universities in
California during his semester leave of last spring.
[July
05]
Year 2004 was very productive
for Dr. Thomas and his
collaborators. They published 11 articles in journals
such as Proceedings of the National Academy of Sciences, Biophysical Journal,
Biochemistry, Journal of Applied Physiology, and Journal of Magnetic Resonance.
[January
05]
Dr. Thomas was appointed William
F. Dietrich Professor in July 2004. The full name of this endowed chair is "William F.
Dietrich Land Grant Chair in Fundamental Molecular/Cell Biology in the Basic
Sciences." In addition, Dr. Thomas has been elected Fellow of the Biophysical Society, the highest honor bestowed by the American
Biophysical Society. He will receive this award officially at the annual BS Meeting
next February in Long Beach. [August 04]
Transition 2004: During the past year, several lab members have
moved on to other positions: congratulations to Josh Baker
(former grad student), who has accepted a position as Assistant Professor at
the
Dr. Thomas and students were featured in the Winter 2003 issue of Bio. See pages 5 (Ben Mueller receives Bloomfield Fellowship.) and 9 (Erika Helgerson and Andrew Jensen help Dr. Thomas pump iron.) BIO, Winter 2003 issue. [January 03]
Structure of Calcium Pump
Regulators: We have used NMR to determine the
structure of sarcolipin, a membrane
protein that regulates the calcium pump in skeletal muscle. This study, a
collaboration between Christine Karim in our lab
and Alessandro Mascioni in Gianluigi
Veglia's lab (Biochemistry, 41: 475-482), involved NMR experiments in
detergent solution as well as solid-state NMR on oriented lipid bilayers.
This is the first high-resolution structure of a calcium pump regulator in its
native lipid environment. The figure at right illustrates hot spots where
mutation affects function. [January 02] More recently, we have used
similar techniques to determine the structure of phospholamban, which regulates the calcium pump in cardiac muscle (Zamoon et al., Biophys J. 2004). [October 04]
Microwave Magic: Yuri Nesmelov (Postdoctoral Research Associate), in collaboration with Jack Surek (grad student), has created a simple device that increases the sensitivity of EPR for small biological samples by an order of magnitude! Yuri did some calculations on the back of an envelope (a very large one) then designed and fabricated a small hollow cylinder of potassium tantalate that focuses the microwave magnetic field onto the sample placed inside it. The device works for samples placed either parallel or perpendicular to the magnetic field, so it should be a big boost to Jack's thesis work on muscle fiber EPR. Read about it in the Journal of Magnetic Resonance, 153: 7–14. 2001. [October 01]
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How Muscle Works: Using EPR of spin-labeled muscle
fibers, we obtained the first direct evidence that the light-chain domain
rotates upon muscle activation (PNAS 95: 2944-2949;
see figure). Using ATP analogs, Ingrid Brust-Mascher,
Leslie Laconte, and Josh
Baker showed that the orientations of the light-chain domain in the pre-
and post-hydrolysis states are not significantly different from each other (Biochem 38: 12607-12613). This surprising result
suggests that the ATP hydrolysis step does not induce a major structural change
in myosin; rather the major stuctural change occurs
upon strong actin binding and phosphate release. [98-99]
View the powerstroke movies (3.1MB) and the 3D rotation movie (1.49MB)
Cardiac Zipper:
Last modified on August 01, 2006