New York Stuctural Biology Discussion Group Winter Meeting 25 Jan 2012
This is the 66th meeting of the Group.
Wednesday, January 25th, 2012, 9:30 – 5:30 Light refreshments served from 9:00 am
7 World Trade Center 250 Greenwich Street, 40th floor Manhattan, NY
This all-day meeting will include presentations by local researchers, lunch, and a poster session.
Dr. Jayne C. Garno receives the prestigious Presidential Early Career Award for Scientists and
Engineers (PECASE) 2010
Dr. Jayne C. Garno, an associate professor of chemistry at Louisiana State University, will receive the prestigious Presidential Early Career Award for Scientists and Engineers (PECASE) this year, the highest honor in the United States for an emerging investigator. Dr. Garno, who is also a recent recipient of the Howard Hughes Medical Institute Distinguished Mentor Award and the Camille Dreyfus Teacher-Scholar Award, credits some of her career success to the help provided by Agilent in getting her instruments up and running quickly as well as assistance in training her students on the latest AFM technologies available for molecular imaging.Dr. Garno earned a B.S. from the University of Michigan and went on to work for General Motors as a bench chemist for 10 years. She then did her advanced degree work and earned a Ph.D. from Wayne State University, serving as a postdoc at Hunter College (City University of New York) and the National Institute of Standards and Technology.As an associate professor at Louisiana State, Dr. Garno teaches both undergraduate students and graduate students. She believes that when undergraduates are given opportunities to interact with professors and be involved with research they develop better awareness of many exciting career paths. Having brought AFM to her own undergraduate students, she is sure that as other departments move into nanoresearch more undergrads will begin to use AFM instrumentation. Dr. Garno encourages her students to present papers at conferences. To date, her students have earned 16 international and national awards. Agilent congratulates Jayne for her contributions to nanoscience research and education.
We plan to join in the 50th-year celebration of the Experimental NMR Conference with a luncheon in Asilomar, March 29-April 4, 2009.
A new grant and a new name for our RCN!
Effective March 1, 2008, the U.S. National Science Foundation funded our RCN, this time with an expanded mission to promote emerging methodologies for molecular structure determination in biological solids. The new network focuses on scanning probe microscopy and cryoelectron microscopy as well as solid-state NMR, both separately and as complementary methods, with the brief moniker of RCN-SCN.
Dr. Marc Baldus receives award
RCN participant Dr. Marc Baldus, a Group Leader at the Max-Planck-Institute for Biophysical Chemistry in Göttingen, has received the Founders Medal of the International Council on Magnetic Resonance in Biological Systems. Check out his research at http://www.mpibpc.mpg.de/abteilungen/030/baldus/
Klaus Gawrisch wins 2007 Avanti Award in Lipids from the Biophysical Society
Klaus Gawrisch wins 2007 Avanti Award in Lipids from the Biophysical Society
Positions Available - Associate Professor and Postdoctoral Associate Institute for Protein Research – Osaka Japan Two positions are available as part of a joint US-Japan research collaboration. One position is at the level of Associate Professor and the other is at the level of Postdoctoral Scientist. Research Projects. Research projects are in the general area of membrane protein structure and function under the guidance of Steven Smith, Professor and Director of Structural Biology, Stony Brook University. See project descriptions below. There will also be considerable opportunity for collaborative research with Japanese scientists.Positions. The positions are part of a reorganization of the Institute for Protein Research in Osaka, Japan. They are funded for 5-years through the Ministry of Education in Japan, and renewable on a yearly basis. Applicants for the position of Associate Professor should have at least 2 years of research experience at the postdoctoral level. Salaries are calculated based on experience, but are in the range of $60-80,000/year (Associate Professor) and $50-$60,000/year (Postdoctoral Scientist). The positions come with a research budget and travel allowance. Institute for Protein Research. The Institute for Protein Research (IPR) is one of the foremost centers for protein research and related science in Japan. The IPR is home to one of the world-wide mirror sites for the Protein Data Bank, and has excellent facilities for structural biology with in-house high-field solid-state NMR and solution-state NMR instrumentation, and access to the Spring-8 beam-line. Contact Information. Send CV and letters of recommendation to Steven O. Smith Center for Structural Biology Stony Brook University Nicolls Rd. Mail Code Z = 5115Stony Brook, NY 11794-5115Phone 631-632-1210Email email@example.comResearch Areas Structure and Activation Mechanism of G protein coupled receptors G protein-coupled receptors (GPCRs) are involved in most cellular processes and are a major pharmaceutical target. On-going projects are to determine the structure of the visual receptor rhodopsin and its photoreaction intermediates. Rhodopsin is the only GPCR whose structure has been determined to high resolution by protein crystallography. The crystal structure corresponds to the inactive, dark-state receptor. We have an established approach for incorporating 13C labels into both the retinal and protein for measurements of internuclear 13C…13C distances using solid-state NMR spectroscopy. Comparison of distances obtained from NMR measurements and from the rhodopsin crystal structure provides validation of the approach. Measurements on the active state of the receptor, are providing exciting new insights into how retinal isomerization is coupled to structural changes within the ‘ligand’ binding site and how these changes result in motion of the transmembrane helices. We are also in the process of extending these studies to several additional class A GPCRs.Patel, A. B., Crocker, E., Eilers, M., Jayararman, S., Hirshfeld, A., Sheves, M. and S. O. Smith (2004) Coupling of retinal isomerization to the activation of rhodopsin. Proc. Natl. Acad. Sci. U.S.A. 101, 10048.Patel, A. B., Crocker, E., Reeves, P, Getmanova, E., Eilers, M., Khorana, H.G. and S. O. Smith (2005) Changes in interhelical hydrogen bonding upon rhodopsin activation. J. Mol. Biol. 347, 803-812.Structure and Inhibition of Amyloid Fibril Formation Amyloid deposits found in neurodegenerative diseases result from misfolding of cellular proteins. The challenge for developing specific inhibitors that block oligomer or fibril formation is that there are no high-resolution molecular structures that can guide the design. Using a combination of high-resolution solid-state NMR and atomic force microscopy (AFM), we are refining the structures that are emerging of oligomers and fibrils associated with Alzheimer’s disease, ‘mad cow’ disease and Parkinson’s disease. Based on the structures that are emerging, we are designing new classes of inhibitors that block fibril formation and reduce the toxicity of protein oligomers and fibrils on neuronal cells. Liu, W., Crocker, E., Zhang, W., Elliott, J. I., Luy, B., Li, H., Aimoto, S. and Smith, S. O. (2004) Structural role of glycine in the formation of amyloid fibrils from transmembrane helices. Biochemistry , 44: 3591.Basic-Aromatic Motifs in Membrane Associated Proteins Unstructured clusters of basic and aromatic residues are a common mechanism for attaching many important proteins to the surface of cell membranes (e.g. Src, K-Ras4B, HIV gag, MARCKS). Recent evidence shows that these clusters are able to selectively bind the phosphoinositide PI(4,5)P2, (or PIP2). Furthermore, there are clues from our recent work that the deep penetration of aromatics may induce the sequestration of cholesterol. On going projects are to establish the molecular mechanism of how basic-aromatic clusters are able to sequester specific lipids into lateral membrane domains, and to determine what happens to the bilayer structure when aromatic residues penetrate the membrane surface. Zhang, W., Crocker, E., McLaughlin and S.O. Smith. (2003) Binding of peptides with basic and aromatic residues to membrane bilayers. J. Biol. Chem. 278, 21459-21466.Gambhir, A., Hangyás-Mihályné, G., Zaitseva, I., Cafiso, D.S., Wang, J., Murray, D., Pentyala, S. N., Smith, S.O. and S. McLaughlin (2004) Electrostatic sequestration of PIP2 on phospholipid membranes by basic/aromatic regions of proteins. Biophysical J. 86, 2188-2207.Transmembrane interactions in receptor tyrosine kinases and cytokine receptors.Cytokine receptors and receptor tyrosine kinases (RTKs) are large integral membrane proteins with single membrane-spanning helices. High-resolution structures have been determined of the ligand binding domain for both classes of receptor, and of the intracellular kinase domain for the RTKs. Structures of the transmembrane and juxtamembrane regions, however, are not available. On-going research is to establish the mechanism for how the transmembrane and juxtamembrane regions couple ligand binding to receptor activation by determining the structure of these regions in their inactive and active conformations. A separate, but related, goal of the research is to understand how viral membrane proteins activate single transmembrane helix receptors in the absence of signaling ligands.Seubert, N., Y. Royer, K. F. Kubatzky, J. Staerk, V. Moucadel, S. Krishnakumar, S. O. Smith and S. N. Constantinescu (2003) Active and inactive orientations of the transmembrane and cytosolic domains of the erythropoietin receptor dimer. Mol. Cell. 12, 1-20.Liu, W., Crocker, E., Constantinescu, S. N. and Smith, S. O. Structure of the transmembrane dimer interface of gp55-p of the spleen focus forming virus. Biophys. J. submitted.
RCN Projects and Plans, Spring, 2005
An overview of the purpose, members, and activities of the RCN was presented by Ruth Stark at UCSD and ENC in March and April of 2005, respectively. More details
The 46th ENC - Experimental Nuclear Magnetic Resonance Conference
Center for NMR Spectroscopy & Imaging of Proteins - Closed
Center for NMR Spectroscopy & Imaging of Proteins The Bubble @UCSD Tuesday, March 15, 2005
12:15 Sign-in, light lunch** 1:00 What is the RCN for NMR of Biological Solids? (R. Stark) 1:05 The NMR Research Resource at UCSD (S. Opella) 1:15 Tailoring NMR Experiments for Oriented Samples (A. Wu) 1:30 NMR Probe Design for Oriented Samples (C. Grant) 1:45 Sample Preparation for Bilayer Samples (F. Marassi) 2:00 Sample preparation for Bicelle Samples (A. de Angelis) 2:15 Laboratory tour and discussions (Hosts)
2005 Eastern Analytical Symposium - Call for paper
Submission of contributed oral and poster presentations for the 2005 EasternAnalytical Symposium will begin on March 7, 2005 and will continue untilApril15, 2005.For more information, please see the EAS web site, http://www.eas.org/
Search capability available on RCN Website
The keyword search capability for postings on RCN website is available.
RCN-NBS Organizational Efforts at 45th ENC
For close to half a century, the Experimental NMR Conference (ENC) has been a meeting place for preeminent researchers focusing on method development and applications for solution, solid, and imaging areas of the field. This year’s ENC in Asilomar, California was the site of the first organizational meeting of the RCN for NMR of Biological Solids. Twenty scientists representing 15 research groups were in attendance at the luncheon gathering; an additional 17 research group leaders affirmed their willingness to join the new group. The NMR researchers came from both academic and governmental laboratories, hailing from the United States, Western Europe, and Japan.