| | Poster judges
- Please score as many of the posters as you can comfortably do in the lunch period.
- Use the NIH like scale 1(best)-9(not best)
- You may or may not reveal that you are judging to the presenter -- your choice.
- please hand your scores to an organizer immediately before the end of the lunch period. If there is space for a private conference of judges, we will try to do that otherwise the organizers will huddle over the scores and do their best.
Poster information
- Your poster should be less than 60" wide, and the top of the panel is at 72" above ground, so you should probably not use more than 42" height.
- You should mount your poster during the first coffee break and dismount it before the second afternoon break.
- Posters not removed by you may be removed by staff, and their condition may be imperfect.
- The judging panel will circulate during the lunch break. Commercial posters and previous winners will not be considered for prizes.
- You may wish to upload your poster to F1000 http://f1000.com/posters . Please indicate it was shown at the Discussion group, referencing our site at http://nysbdg.org
Posters list
- Mary E. Heavner, Gwenaelle Gueguen, Shaneen Singh, and Shubha Govind ; Institutions: CUNY: Graduate Center, The City College, and Brooklyn College ; Title: The Computational Structural Analyses of Two Potentially Significant Proteins from the Virus-Like Particles (VLPs) of Parasitoid Wasp Leptopilina heterotoma
- Rhodora Cristina Calizo ; Poster Title: Studies of the Bradykinin 2 and mu-Opioid Receptors Suggest that Caveolae Localization of GPCRs is Mediated by their Attached G proteins ; Lab: Suzanne Scarlata ; Department of Physiology & Biophysics, Stony Brook University, Stony Brook, NY 11794-8661, USA ; ABSTRACT ; Caveolae are membrane domains that may influence cell signaling by sequestering specific proteins such as G protein coupled receptors (GPCRs). While previous reports largely show that Gαq, but not other G proteins, interact strongly with the caveolae protein, Caveolin-1, the inclusion of GPCRs in caveolae is controversial. Here, we have used fluorescence methods to determine the effect of caveolae on the physical and functional properties of two GPCRs that have been reported to reside in caveolae, the bradykinin receptor type 2 (B2R), which is coupled to Gαq, and the µ opioid receptor (µOR), which is coupled to Gαi. While caveolae do not affect cAMP signals mediated by µOR, they prolong Ca2+ signals mediated by B2R. Immunofluorescence and Förster Resonance Energy Transfer (FRET) studies show that a significant fraction of B2R resides at or close to caveolae domains while diffusion measurements indicate they reside in the periphery rather than inside the domains. FRET between B2R and caveolae is reduced by down-regulation of Gαq or by addition of a peptide that interferes with Gαq /caveolin-1 interactions suggesting that Gαq promotes localization of B2R to the periphery of caveolae. Additionally, down-regulating endogenous Cav1 in A10 cells ablates the prolonged Ca2+recovery seen upon bradykinin stimulation in accord with the idea that the presence of caveolae prolongs Gαq activation. Taken together, our results suggest that Gαq can localize its associated receptors to the periphery of caveolae to prolong enhance their signals.
- Griselda Hernández ; Title: Experimentally Assessing Molecular Dynamics Sampling of the Protein Native State Conformational Distribution ; Authors: Griselda Hernández1, Janet S. Anderson2, David M. LeMaster1? ; Institution: Wadsworth Center, New York State Department of Health1, Union College2
- Igor Dikiy, David Eliezer - WMCCU - NMR characterization of N-terminally acetylated alpha-synuclein in E coli cells and in vitro ; Abstract - N-terminal acetylation of alpha-synuclein has recently gained widespread attention as a post-translational modification of this protein in mammalian cells that might alter its structural properties when compared with the unacetylated recombinant protein that has been used for nearly all previous studies of synuclein structure. We show that alpha-synuclein is quantitatively N-terminally acetylated in E. coli transfected with the yeast NatB? acetylation complex. We use NMR spectroscopy to characterize the structural properties of N-acetylated alpha-synuclein after purification, in fresh cell lysates, and in intact cells. We find that N-terminal acetylation increases the transient helical propensity of the first ~10 residues of purified recombinant alpha-synuclein but does not otherwise alter the intrinsically disordered nature of the protein. Previously characterized transient long-range contacts in the protein are also not substantively altered, and the protein remains monomeric. Spectra obtained in freshly lysed cells without further purification are identical to those of the fully purified protein. Finally, spectra of N-terminally acetylated and unacetylated alpha-synuclein in intact cells are identical. Although the first 10 residues of the protein, which is the region where the effects of N-terminal acetylation can be observed, do not give rise to observable resonances in intact cells, our results clearly show that that N-terminal acetylation does not dramatically alter the structure or oligomerization state of alpha-synuclein in this context.
- Rejwan, Ali; Monte Carlo Loop Refinement of Trans-Membrane Domain of the Thyroid Stimulating Hormone Receptor ; Rejwan Ali, Rauf Latif, Terry Davies and Mihaly Mezei ; Mount Sinai School of Medicine and James J. Peters Veterans Affairs Medical Center, New York, NY
- Mariena Silvestry Ramos ; Name: CEM Staff at NYSBC ; Institution: New York Structural Biology Center ; Title: Cryoelectron Microscopy Facility at the NYSBC
- Shula Shazman 1,2,3, Jie Chen 1,2,3, Hunjoong Lee 1,2,3, Richard Mann ; 1,Barry Honig 1,2,3 ; INSTITUTIONS: 1: Department of Biochemistry and Molecular Biophysics, Columbia ; University, New York; 2: Center for Computational Biology and Bioinformatics, Columbia ; University, New York; 3: Howard Hughes Medical Institute; TITLE: On The Fly ? A Database of Drosophila Melanogaster Transcription Factors (TF) and TF Binding Sites
- Paul Galatis ; Pfizer ; Moving Into Terra Incognita – Expanding the Frontiers of LRRK2 Biology using potent, selective, brain penetrant and in vivo active tool compounds
- previous winner, not for judging Sozanne Solmaz, Radha Chauhan, Gunter Blobel and Ivo Melcak. ; HHMI at the Rockefeller University, 1230 York Ave, New York NY 10065. ; Large diameter changes of the transport channel of the nuclear pore complex.
- Yu Zhang ; Institution: Waksman Institute, Rutgers University ; Title: Structure basis of transcription initiation
- Muhamed Amin ; Institution: CUNY ; Title: "Computational approach to study the structure/function of metalloenzymes"
- Garrett Katz ; Protein P7: A Molecular Bracket in the Cystovirus f6 Procapsid ; Garrett Katz1, Hui Wei1, Alexandra Alimova1, A. Katz2, David Gene Morgan3 and Paul Gottlieb1* ; 1Sophie Davis School of Biomedical Education, City College of New York, New York, NY 10031, USA. ; 2Department of Physics, City College of New York, New York, NY 10031, USA ; 3Chemistry Department, Indiana University, Bloomington, IN 47405, USA.
- Dipankar Roy, Gábor Pohl, Jorge Ali-Torres, Mateusz Marianski, and Joseph J. Dannenberg ; Institution: City University of New York - Hunter College and the Graduate School ; Title: Density Functional Theory (DFT) study of -Hairpins in Antiparallel -Sheets, A New Classification Based upon H-bond Topology.
- Gheevarghese Raju & Ronald l koder, City College of New York, Title: De Novo Designed Safranine Enzymes.
- Romina Mancusso "Structure and mechanism of a bacterial sodium-dependent dicarboxylate transporter" ; Authors: Romina Mancusso, G. Glenn Gregorio, Qun Liu and Da-Neng Wang. Institutions: Skirball Institute of Biomolecular Medicine, New York University. New York Structural Biology Center, NSLS X4, Brookhaven
- Huang, Wenlin ; Title: Studying Suberization in Potato Tuber Periderms Using NMR- and MS-based Metabolomics ; Name: Huang, Wenlin ; Institution: Department of Chemistry, The City College of New York and CUNY ; Institute for Macromolecular Assemblies, New York, NY 10031
- Milena Popović and Nancy L. Greenbaum ; Hunter College of CUNY ; "Structuring of a guide sequence located within the ID3 stem loop upon binding of its target Exon 1 sequence in S. cerevisiae group II intron"
- Evgeniya Rubin "Protein Crystallization under Electric Fields". BNL
- commercial not for judging Robert Newman "Innovations in SBS-format microplates for high throughput protein crystallization and diffraction screening" MiTeGen?, Ithaca
- ANUSHI SHARMA ; POSTER TITLE:UNDERSTANDING THE KINETIC MECHANISM OF MUTS DNA MISMATCH REPAIR PROTEIN ; NAMES: ANUSHI SHARMA, MANJU HINGORANI ; WESLEYAN UNIVERSITY, MIDDLETOWN, CT
- Name: Zhizhen Jane Zhao ; Institution: Princeton University ; Title: Rotationally Invariant Image Representation for Viewing Angle Classification in Cryo-EM ; Abstract: We introduce a new rotationally invariant viewing angle classification method for identifying, among a large number of Cryo-EM projection images, similar views without prior knowledge of the molecule. Our rotationally invariant features are based on the bispectrum. Each image is first expanded in an orthonormal steerable basis to generate expansion coefficients. Rotating an image is equivalent to phase shifting the expansion coefficients. Thus we are able to extend the theory of bispectrum of 1D periodic signals to 2D images. The randomized PCA algorithm is then used to efficiently reduce the dimensionality of the bispectrum coefficients, enabling fast computation of the similarity between any pair of images. The nearest neighbors provide an initial classification of similar viewing angles. In this way, rotational alignment is only performed for images with their nearest neighbors. The initial nearest neighbor classification and alignment are further improved by a new classification method called vector diffusion map.
- Rong Xu, Dongsheng Liu, David Cowburn, Einstein Coll Med, "Segmental isotopic labeling of protein tyrosine kinases"
- I. A. Kriksunov, R. Cerione, M. Cook, R. Gillilan, Q. Huang, C. U. Kim, W. Miller, D. Schuller, S. Smith, S. M. Gruner & D. M. E. Szebenyi ; MacCHESS?: serving structural biology. ; MacCHESS?, Cornell University, Ithaca, New York 14853, USA ; Abstract: MacCHESS? is a facility supporting Macromolecular diffraction at CHESS, the Cornell High Energy Synchrotron Source. Funded by the National Institutes of Health's NIGMS program, MacCHESS? is charged with both providing state-of-the-art support for experiments with macromolecules– crystallography, SAXS, and more – and pursuing research initiatives designed to benefit both CHESS users and the wider structural biology community.
- Deepa Rajasekaran ; Yale Med ; Title A MODEL OF GAG:MIP-2:CXCR2 INTERFACES AND ITS FUNCTIONAL EFFECTS ; Abstract - MIP-2/CXCL2 is a murine chemokine with Glu-Leu-Arg (ELR) activation motif and activates CXCR2 for neutrophil chemotaxis1. We determined the structure of MIP-2 to 1.9Ĺ resolution and created a model with its receptor murine CXCR2 based on the coordinates of human CXCR42. Chemokine-induced migration of cells through specific G protein-coupled receptors is regulated by glycosaminoglycans (GAGs) that oligomerize chemokines3. MIP-2 GAG-binding residues were identified that interact with heparin disaccharide I-S by NMR spectroscopy. A model a GAG:MIP-2:CXCR2 complex that supports a 2:2 complex between chemokine and receptor was created. Mutants of these disaccharide-binding residues were made and tested for heparin binding, in vitro neutrophil chemotaxis, and in vivo neutrophil recruitment to the mouse peritoneum and lung. The mutants have a 10-fold decrease in neutrophil chemotaxis in vitro. There is no difference in neutrophil recruitment between wild-type MIP-2 and mutants in the peritoneum but all activity of the mutants is lost in the lung supporting the concept that GAG regulation of chemokines is tissue-dependent.
- VLADIMIR VIGDOROVICH(a), Udupi A. Ramagopal(b), Steven C. Almo(bc), Stanley G. Nathenson(ad) TITLE: Structure and multimerization properties of a T cell activity modulating signal molecule, B7H3. INSTITUTIONS: (a) Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York (b) Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York (c) Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York (d) Department of Cell Biology, Albert Einstein College of Medicine, Bronx, New York
- Yogesh Gupta (Aneel Aggarwal's Group) Structural Insights into the Assembly and Shape of Type III Restriction-Modification (R-M) EcoP15I? Complex by Small-Angle X-ray Scattering ; Mount Sinai School of Medicine, New York.
- Yayan (first name ), Zhou(last name) ; Institute: MB&B department, Wesleyan University (graduate student from Prof. Manju Hingorani's lab) ; Poster name: Impact of Individual PCNA-DNA contacts on clamp loading and function on DNA.
- David Snead, David Eliezer ; WMCCU ; "Characterization and functional relevance of complexin C-terminal domain lipid interactions." ;ABSTRACT: The presynaptic protein complexin modulates both spontaneous and stimulus-evoked SNARE-mediated vesicle fusion, with distinct domains either facilitating or inhibiting exocytosis. Complexin’s C-terminal domain (CTD) inhibits spontaneous fusion in worm, fly, and mouse through an as yet unknown molecular mechanism. Using solution nuclear magnetic resonance spectroscopy, we show that worm complexin’s CTD is predominantly disordered with a slight helical propensity. Interestingly, the CTD binds to negatively charged large unilamellar vesicles (LUVs) in a salt dependent manner, but not to neutral LUVs, implying a significant role for electrostatic interactions. Deleting the CTD alters complexin’s mobility at the synapse. We identify a novel lipid binding region at the very C-terminus of complexin’s CTD and a previously noted amphipathic region as participating directly in lipid binding. A double LV/EE mutation in the amphipathic region disrupts lipid binding, and both the LV/EE mutation and deletion of the C-terminal 12 residues impair its inhibitory activity in functional assays of synaptic activity in living worms.
- Ying Li (presenting author) Full Author list: Ying Li, Nicole Altorelli, Fabiana Bahna, Barry Honig, Lawrence Shapiro, Arthur Palmer ; Columbia University Department of Biochemistry and Molecular Biophysics ; Title: An intermediate state in epithelial cadherin dimerization pathway detected by NMR relaxation dispersion
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