Albany 2011: Conversation 17
June 14-18 2011
©Adenine Press (2010)
Topics, Speakers, Chairs and Guests
The 17th Conversation, June 14-18, 2011 will be held at the State University of New York, Albany, NY 12222 USA. Participants will arrive on Tuesday June 14th, there is a reception that evening. The scientific program starts Wednesday morning June 15th and will end after lunch on Saturday June 18th at 2:00 PM. The conference will have roughly 50 lectures by leading scientists, in addition to several short lectures by young scientists who will be selected from abstracts submitted for poster presentations. We will have on display, throughout the conference, some 250 posters. We anticipate about 400 participants with diverse background from over 20 countries for these continuing conversations.
Young Scientists Lecture Program
The Organizing Committee has left 5.5 hrs of the Conversation time for the young scientists lecture program. Extraordinarily talented young professional researchers, at the rank of assistant professors, post-doctoral fellows and doctoral students, will be selected from the abstracts submitted for lecture + poster presentations to provide oral presentations which will be sandwiched between those by senior scientists. Go to link in the sidebar.
Ramaswamy H. Sarma, Department of Chemistry
State University of New York, Albany NY 12222 USA
ph: 518-456-9362; fx: 518-452-4955; email:email@example.com
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200 Page Book of Abstracts in PDF: Print Version
Detailed Schedule of 17th Conversation
Abstracts: Requirements & Deadlines
Registration, Meals and Accommodation
Young Scientists Speaker Program
17th Conversation Poster
Book of Abstracts: Albany 2011
Department of Biology
Office of the Dean, Arts and Sciences
Office of the Vice President for Research
The Albany Conversation traditionally holds evening lectures in areas of fundamental interest to structural biology. In 2011, on Wednesday June 15th 8:00 PM, Nobel Laureate Jack W. Szostak, Alexander Rich Professor of Molecular Biology, Harvard Medical School, will provide a lecture on the laboratory synthesis of self-replicating systems and the origin of life. The development of non-enzymatic replication systems is a major challenge in the fields of nucleic acids chemistry and the origin of life. Professor Szostak will describe recent experiments with three different phosphoramidate-linked nucleic acids that bring us closer to the realization of a general template-directed copying chemistry. In addition, Prof. Szostak will discuss the compatibility of these systems with a protocell-membrane replication system, and progress towards the design of a complete self-replicating protocell. Prof. Alexander Rich, MIT, will introduce Professor Szostak and chair the session.
Proteins: What is New, Newer and Newest?
The mechanism of how proteins fold, which is at the center of a number of problems in biology, continues to be a challenging problem. Dave Thirumalai, University of Maryland, presents new theoretical advances in predicting the folding pathways of proteins. The calculations done at exactly the experimental conditions, afford us for the first time, to make quantitative comparisons with single molecule experiments. Angel Garcia, Rensselaer Polytechnic Institute, using Trp-cage miniprotein as an example, shows how molecular dynamics allow us to make detailed calculations of the thermodynamics of folding/unfolding over a broad range of temperatures, co-solvent, and pressures, providing atomistic details of the effects of pressure and co-solvents on the folded and unfolded state ensembles. B. Jayaram, Indian Institute of Technology, New Delhi, India, will show how Stoichiometry Driven Margin of Life Leads to a Universal Spatial Organization of Backbones of Folded Proteins. In search of common principles underlying the magnificent diversity in folded proteins, Jayaram and Mittal conducted rigorous analyses of several thousands of protein crystal structures. These assumption-free analyses reveal a surprisingly simple stoichiometry driven unifying principle of backbone organization of folded proteins regardless of their size, shape and sequence. A critical appraisal on the implications of their findings to protein architectures will be presented. Ken Dill, University of California San Francisco, provides insights into cellular level proteostasis, and shows how certain properties of protein stability and aggregation can be predicted without supercomputers. Irit Sagi, Weizmann Institute, Israel, advances structural–kinetic experimental approaches to investigate matrix metalloenzymes at atomic details and in real-time. Her experimental approach allows the elucidation of the structure and chemistry of reactive transient species that could not be detected by conventional tools. The fine mechanistic information derived using this experimental strategy is currently being used to provide insights and new leads to the design of drugs in the form of function blocking antibodies targeted at metalloenzyme catalytic sites. What is the newest in NMR for proteins is taken up by David Cowburn, Albert Einstein College of Medicine. Systematic approaches to the structural features of protein interfaces require new methodological developments in NMR, prioritized by leading edge systems of practical biological interest. Challenges include how to characterize intrinsically disordered segments, and closer approach to the intracellular environment than that provided by conventional solution methods. Cowburn illustrates recent progress in these areas combining NMR measurements with extensive protein engineering, with small angle scattering methods, and with in cell interaction approaches.
Proteins: Allostery, Cooperativity and Motion
Chaperonins are molecular machines that undergo large-scale ATP-driven conformational changes that are crucial for their protein folding function. These changes are concerted in the case of the prokaryotic chaperonin GroEL and sequential in the case of the eukaryotic chaperonin CCT. Amnon Horovitz, Weizmann Institute, Israel, will describe experiments and lattice model simulations that explore the implications of these different allosteric mechanisms for the folding function of chaperonins. The use of atomistic simulation techniques to directly resolve protein tertiary structure from primary amino acid sequence is hindered by the rough topology of the protein free energy surface and the resulting simulation timescales required. Richard Bryce, Univ. of Manchester, UK, will discuss his work on developing computational techniques, based on cooperative multicopy molecular dynamics simulations, to address these challenges. The cooperative molecular dynamics strategy shows enhanced prediction of peptide and protein conformation in aqueous solution. Ivet Bahar, Univ. of Pittsburgh, is using elastic network models (ENMs) for understanding the collective machinery of large molecular systems. ENMs permit us to efficiently evaluate the global (or softest) modes of motions accessible to biomolecular systems near native state conditions. Comparison with experimental data demonstrates that these modes are exploited by proteins in many functional interactions, including protein-protein and protein-ligand recognition and binding.
Intrinsically Disordered Proteins and Neurodegeneration
Intrinsically disordered proteins (IDPs) perform essential functions in organisms from all phyla and their improper functioning is responsible for numerous disease states in humans, including some cancers and neurodegenerative diseases. IDPs populate broad conformational ensembles that are characterized by molecular motions on multiple timescales but it remains unclear whether random polymer models reliably describe these ensembles or whether new models are necessary. In order to develop general relationships between the structure and function of IDPs, Gary Daughdrill, Univ. South Florida, is investigating the structure and dynamics for a family of proteins that are intrinsically disordered. The work is being placed in an evolutionary context to permit an assessment of important structural features by virtue of their conservation and constitutes the first attempt to quantify the relationship between sequence identity and structural similarity for IDPs. David Eliezer, Cornell Univ., takes up alpha-synuclein and tau protein which are intimately linked to the etiology of Parkinson's and Alzheimer's diseases, yet neither protein adopts a well-defined structure when isolated in solution. Magnetic resonance studies of both proteins inform on the structural transitions that they undergo in different contexts, and lead to hypothesis regarding both their normal function and pathology. Akihiko Takashima, RIKEN, Saitama, Japan, devotes his talk entirely to Alzheimer's disease. He sees Neurofibrillary tangles (NFTs), composed of highly phosphorylated tau in tauopathies such as Alzheimer's disease. Tau is a microtubule-associated protein and is an IDP. The process of NFT formation induces synapse loss and neuronal loss, leading to brain dysfunction. During NFT formation tau forms soluble oligomer tau, granular tau oligomer and tau fibril. Takashima will report the role of each tau aggregate in neurodegeneration.
For some time now, a basic universal structural element of globular proteins, closed loops with a characteristic size 25-30 residues and ring-like shape, has been advocated by Igor Berezovsky, University of Bergen, Norway. Elementary functional loops (EFL) have specific signatures and provide functional residues important for binding/activation and principal chemical transformation steps of the enzymatic reaction. The existence of EFLs in different folds and functions makes it possible to survey subtle evolutionary relations, originating from the pre-domain evolution of protein structure. It suggests that contemporary enzymatic functions are constructs of different sets and combinations of elementary chemical functions. An exhaustive description of a protein fold and its enzymatic function as a combination of EFLs illuminates how this fold emerged in pre-domain evolution by fusion of prototype genes. William Duax, Hauptman-Woodward Institute, examines the evolution of ribosomal proteins. An alignment of all 1850 copies of each bacterial ribosomal protein in the gene bank, based upon 100% conservation of specific residues including Gly, Ala, Arg, and Pro (GARP) residues critical to the folds of each ribosomal protein, can be used to identify positions where specific residues (i) separate Gram positive from Gram negative bacteria and (ii) co-isolate cyanobacteria and chloroplasts. The sequence differences in ribosomal proteins that separate different phyla, classes, and orders of bacteria can potentially be exploited in the design of antibiotics that will selectively inhibit the growth and survival of specific bacterial genera. Loren Williams, Georgia Tech, will describe how to use the ribosome as a molecular time machine. The ribosome contains the oldest macromolecules in biology, dating from well before the first branch point in the tree of life. Williams uses the ribosome to help reconstruct and resurrect ancient biochemistry and assembly.
Breakthroughs in Molecular Simulations
Molecular simulations have come to play the role of a computational microscope that permits novel discoveries. Klaus Schulten, Univ. of Illinois, U-C, will describe how breakthroughs in simulation speed, size and multi-resolution methodology permit today atomic level views of dynamic molecular machines the size of the ribosome. To make his point, he will present from joint experimental and simulation approaches snapshots of the difference of initiation and elongation tRNAs acting in the ribosome, of a nascent protein that regulates the ribosome, and even of a nascent protein being weaved into a lipid bilayer in a ribosome - SecY complex. Ruxandra Dima, Univ. of Cincinnati, will discuss how combining the power of graphics cards with novel computational modeling techniques allows for the probing of the mechanical behavior of large biomolecular assemblies on timescales characteristic for single-molecule experiments. Gianni De Fabritiis, Univ. Pompeu Fabra, Barcelona, Spain, uses molecular dynamics on GPUs to reveal the process of protein-protein interaction directly and in particular protein-ligand binding. David Beveridge, Wesleyan Univ., will present validations and assessments of molecular dynamics on DNA based on millisecond trajectories. Results on sequence effects on dynamical structure, ion atmosphere, DNA bending and flexibility, and trajectory analyses based on PCA free energy landscapes will be presented and discussed.
Evolution: Prebiotic Synthesis
We are witnessing today many sensational moves towards “creation” - exploration of artificial designs conspicuously close to the hypothetical scenario of origin of life. It is the thesis of Edward N. Trifonov, University of Haifa, Israel, that, although the phenomenon of life, actually, does not have yet a definition agreed upon, one has a strong feeling that we are very close to the origin (of exactly what?). Perhaps, even beyond the uncertain point of the nonlife-to-life transition. Is the hunted watching our backs? And could not life, after all, originate in the outer space? Uwe Meierhenrich, University of Nice-Sophia Antipolis in France, has produced some microgram of an artificial comet, in which a wide variety of amino acid structures were detected. These amino acids and diamino acids will be discussed with respect to both the origin of life on Earth and the chirality of proteinogenic amino acids. Ernesto Di Mauro, University of Rome, Italy, ponders on the emergence of pre-genetic Information; he advocates the theory that HCN/formamide provides a plausible unitary frame for the origin of the genetic polymers in the extant forms of life on planet Earth. James Ferris, Rensselaer Polytechnic Inst., will report on progress in the montmorillonite clay-catalyzed condensation of activated nucleotides of adenosine and uridine to form RNA oligomers to serve the RNA world of origin of life. And finally Nick Hud, Georgia Tech, takes up the pre RNA world. His studies are directed towards understanding which informational polymers could have preceded RNA in the earliest stages of life, the “midwife” molecules and solvent conditions that could have facilitated the polymerization of pre-RNA.
Chromosomes - Landscape of the Cell Nucleus
Evidence from a multitude of approaches indicate the cell nucleus as a dynamic landscape harboring chromatin and non-chromatin nuclear structures, including chromosome territories, chromatin domains and loops, genes, nuclear bodies, splicing speckles as well as molecular machineries that orchestrate transcription, co-transcriptional splicing, as well as DNA replication and repair. Thomas Cremer, LMU Biozentrum, Martinsried, Germany, will examine functional nuclear architecture characteristics and the topography of transcription using super-resolution light microscopy (breaking the Abbe limit). Kazuhiro Maeshima, National Institute of Genetics, Mishima, Japan, looks into compaction of long strands of DNA into a mitotic chromosome and shows that mitotic chromosomes essentially consist of irregular folding of nucleosome fibers without regular hierarchical structures like 30-nm chromatin fibers. Jonathan Widom, Northwestern Univ., observes: Genomes ranging from histone-containing archaea to man appear to explicitly encode aspects of their own organization into nucleosomes. He is working to elucidate the sequence rules and physical principles that govern this organization, and to understand how genomes utilize this novel information to facilitate chromosome function.
Artificial DNA from a PNA (peptide nucleic acid) perspective will be taken up by Peter E. Nielsen, Univ. of Copenhagen, DK - implications for & applications in (chemical) biology & drug discovery: What do we learn from artificial DNA? What can we use it for? These are some of the questions Dr. Nielson asks. Maxim Frank-Kameneskii, Boston Univ., will cover targeting of duplex DNA using artificial DNA. Triplex forming bis-PNAs have excellent sequence discrimination & form very stable complexes with dsDNA but they have sequence limitations. Using the recently introduced gamma-PNA carrying G-clamp the sequence limitations have been lifted. Various applications of the dsDNA targeting by bis-PNA & by gamma-PNA will be discussed.
The most important results in structural DNA nanotechnology involve the control of structure in 3D. Recently Ned Seeman, New York Univ., has self-assembled crystals of multiple robust DNA motifs that diffract to 4-5 Å resolution. By attaching different dyes to the DNA motifs, he can control the colors of the crystals. In addition, Ned has recently been able to combine a variety of DNA nanomechanical components to make a programmable DNA-based nanomechanical assembly line. A unique walker has been designed to travel along a DNA origami that contains three stations. The three stations contain 2-state DNA devices, each associated with a cassette to embed it into the origami; the devices are attached to unique cargoes, which consist of a variety of gold nanoparticles. The devices themselves can be programmed to donate their cargoes or not to donate their cargoes to the walker as it traverses a path on the origami. Thus, Ned can use the same system to produce eight different products, as a function of the programming of the system.Kurt Vesterager Gothelf, Aarhus Univ., Denmark, deals with one of the greatest challenges in nanotechnology, viz., to control the positioning of building blocks at the nanoscale. He uses the unique programmability of DNA and his knowledge to modify DNA to form complex nanostructures with well-defined geometry. Friedrich Simmel, Technische Universität München, Germany, uses the unique molecular recognition properties of DNA to build static and dynamic molecular structures. He discusses how machine-like, switchable molecular structures can be made from DNA and RNA molecules, and how they can be used as components of artificial biochemical reaction networks.
Since his discovery of Z-DNA back in 1979, Alex Rich, Mass. Institute of Technology, has been exploring the biological role of Z-DNA and proteins that bind to Z-DNA. At the 2011 Conversation Alex Rich will elaborate on the role of these proteins in pox virus infection, and the progress one has made in developing a therapy for these infections. He will also present the role of Z-DNA binding proteins in innate immune systems. Martha Bulyk, Harvard Medical School, advocates the thesis that the interactions between sequence specific transcription factors (TFs) and DNA binding sites are part of the regulatory networks within cells. Using the universal protein binding microarrays developed in her lab, she has determined the DNA binding specificities of over 500 TFs from a wide range of species, thus illuminating on novel TFs, tissue-specific transcriptional enhancers, functional divergence of paralogous TFs within a TF family, and the molecular determinants of TF-DNA 'recognition' specificity. Christoph W. Müller, European Molecular Biology Laboratory, Heidelberg, Germany, talks about the cooperative binding of multiple factors to adjacent DNA sites and the interactions of sequence-specificTFs with co-activators and general transcription factors. Using coarse-grained models, Koby Levy, Weizmann, Israel, visualizes protein sliding along DNA, and explores the interplay between the protein characteristics (e.g., DNA recognition motifs, degree of flexibility, oligomeric states, and cross-talks between domains) and the nature of sliding, inter-segment transfer events and the overall efficiency of the DNA search. Remo Rohs, University of Southern California, will outline two different ways of modulating DNA shape, as a function of nucleotide sequence or as a variation in base pairing geometry, that contribute to specific interactions of arginine residues with DNA binding sites of a variety of protein families. The nuances and complexities of recognition in specific cases such as p53 tumor suppressor protein, C2H2 zinc fingers and homeodomains, single-stranded RNA and DNA by cold shock domains, will be addressed by Zippi Shakked, Weizmann Institute, Israel, Scot Wolfe, University of Mass. Medical School, Worcester, and Udo Heinemann, Max Delbrueck Center for Molecular Medicine, Berlin, Germany. With surgical precision, brick by brick, Victor Zhurkin, National Institutes of Health, delineates, the intimate details of the DNA trajectory and deformation during DNA-histone rendezvous to position nucleosomes.
Cis-regulatory modules (CRM) are segments of DNA responsible for tissue-and time-specific regulation of gene expression. In multicellular eukaryotes CRMs may be located not only in the upstream vicinity of the transcription start sites of the controlled genes, but also can be away by tens of thousands of nucleotides from transcription start sites, both upstream and downstream. CRMs make an important component of meaningful non-coding DNA. CRMs contain multiple binding sites for protein factors regulating the transcription. Identification of CRMs in silico and prediction of their regulatory function allows one to suggest new regulatory inputs controlling expression of particular genes, which makes a useful introductory step before modeling of cellular processes. Genetic variations overlapping with CRMs contribute to functional disorders associated with non-coding DNA. Several related aspects of CRM modules will be addresed by Vsevolod Makeev, GosNIIGenetika, Moscow, Russia, Alexander Kel, GeneXplain GmbH, Wolfenbuttel, Germany and Olga Ozoline, RAS, Pushchino, Russia. The talks describe potential and difficulties of identification of CRM location and function in silico in several model systems; an example of application of composite promoter analysis for causal interpretation of cancer gene expression data, which helps to reconstruct gene regulatory network and detect key regulatory nodes, leading to identification and validation of novel drug targets; possible biological role of novel genomic elements on the basis of experimental data, reflecting their unusual functional properties (probing in vitro, in vivo and in situ) and data obtained by comparative genomics.
DNA Damage and Repairs
DNA repair machines keep DNA damage from disrupting transcription and replication and prevent double-strand breaks from becoming chromosome breaks by tethering the DNA ends and by orchestrating signaling and repair responses. John A. Tainer, Scripps, will focus his talk on "Dynamic XPD & Mre11-Rad50-Nbs1 DNA repair complexes". XPD in the TFIIH transcription-repair complex and Rad50 in the Mre11-Rad50-Nbs1 complex connect DNA repair machinery to biological outcomes by long-range allosteric changes that are being elucidated by combined structural and genetic results. DNA repair enzymes face a difficult task of finding rare DNA lesions among a vast excess of undamaged DNA. Dmitry Zharkov, SB RAS Institute of Chemical Biology, Novosibirsk, Russia, elaborates on the mechanisms to facilitate lesion search that rely on the reduction in the dimensionality of the search and a multi-stage nature of damaged base discrimination. In the past decade, we have learned that humans have ten DNA cytidine deaminases that catalyze a variety of physiological functions from triggering antibody gene diversification to preventing the replication of a wide array of retrotransposons and retroviruses. Reuben S. Harris, Univ. of Minnesota, will discuss recent advances in the biochemistry and structural biology of these enzymes that help us to better appreciate their cellular functions. Vittorio Enrico Avvedimento, Università Federico II di Napoli, takes up the good and bad of DNA damage: DNA oxidation drives transcription initiation. The estrogen and retinoic acid bind to their cognate nuclear receptors, penetrate into chromatin and bind specific DNA sequences in the genome, and ultimately set off an oxidation wave that modifies the DNA locally and recruits the enzymes, involved in base excision repair. Finally Mike Fried, Univ. of Kentucky, takes up alkylation. Human cells contain DNA alkyltransferases that protect genomic integrity under normal conditions but also defend tumor cells against chemotherapeutic alkylating agents. Here we explore how structural features of the DNA substrate affect the binding and repair activities of the human O6-alkylguanine-DNA alkyltransferase, with the aim of understanding its mechanisms and possibly developing mechanism-based inhibitors for use in cancer chemotherapy.
The history of these transcription-replication collisions discovered in 1988 will be reviewed by Sergei Mirkin, Tufts University, in addition to elaborating on replication blockage upon co-directional collision with the RNA polymerase stalled due to the R-loop formation. Benedicte Michel, CNRS, Gif-sur-Yvette, France, reports on the reactions that take place in E. coli at replication forks inactivated by a collision with transcription. He describes three bacterial helicases which assist replication across oppositely-oriented, highly-transcribed regions, and recombination proteins that participate in the replication restart reaction. Jorge B. Schvartzman, CSIC, Madrid, Spain, takes up bacterial plasmids which must be negatively supercoiled to initiate DNA replication. In addition, as replication proceeds, sister duplexes get intertwined and may contain intramolecular knots in the replicated portion. In his lab, they use E. coli mutants, Two-Dimensional agarose gel electrophoresis and Atomic Force Microscopy to reveal the roles of DNA gyrase and topoisomerase IV as the topology of DNA changes during replication. Michael O'Donnel, Rockefeller University, summarizes recent advances on how the replisome deals with DNA lesions, proteins bound to DNA, and transcribing RNA polymerase. Single -molecule studies will describe investigations into another type of barrier - the opposite directionality of the lagging strand relative to the direction of the chromosome. Sue Jinks-Robertson, Duke University, finds that high levels of transcription elevates mutation rates in budding yeast, primarily because of an accumulation of transcription-associated DNA damage. Genetic studies reveal two novel sources of this DNA damage: (1) enhanced activity of topoisomerase I and (2) alterations in the base composition of the DNA template.
David Beveridge, Wesleyan Univ., has been with the Albany Conversation since its inception in 1979 when he was at Hunter College, New York City. Albany Conversation is delighted to celebrate his achievements along with his students and colleagues. This scientific session features some of his former and present students. Mihaly Mezei, Mount Sinai Schl. of Medicine, will discuss application of concepts developed while he was working in the Beveridge Laboratiory. Grand-canonical ensemble simulations were shown to be well suited for the exploration of solvent occupancy of isolated pockets inside macromolecules. From the ensemble of configurations thus generated, the concept of generic sites serves to identify distinct water sites inside proteins. Matthew Young, Univ. of Michigan, focuses on protein kinases which represent one of the fundamental components of cell signaling networks that function as switches to propagate signals in a tightly regulated fashion. He is using x-ray crystallography and computational methods to characterize the catalytic mechanism of CDK2 kinase and investigate how the signaling activity of this enzyme can be regulated by external influences. Na Le Dang, Wesleyan Univ., is interested in the driving forces, the kinetics and thermodynamics involved in the transient states of protein-RNA binding reactions. Explicit-solvent Molecular Dynamic, coarse-grained Monte-Carlo Metropolis simulations are performed on different protein-RNA complexes to construct the energy landscapes. Ishita Mukerji, Wesleyan Univ., will dwell on structure and dynamics of DNA Four-Way Junctions complexed with proteins, emphasizing the recent experimental and computational work. The transition from the open form to the ion-induced stacked form, particularly with respect to the overall dynamics of the junction and the location of ions, will be highlighted. Finally, Elizabeth Wheatley, Wesleyan Univ., will present a molecular dynamics simulation-based study of DNA Holliday Junctions, focusing on elucidating conformational stability and junction transitions.
Chairs of Sessions
Valeri Barsegov, Univ. of Mass, Lowell
Elena Bichenkova, Univ. of Manchester, UK;
Tom Bishop, Tulane University
Thomas Cheatham, University of Utah
Rick Cunningham, SUNY at Albany
Dan Fabris, SUNY at Albany
Miroslav Fojta, Institute of Biophysics, Czech Republic
Mikhail Gelfand, IITP, Moscow, Russia
Manju Hingorani, Wesleyan Univ.
Barry Honig, Columbia Univ.
Neville Kallenbach, New York Univ.
Richard Mann, Columbia Univ.
Aditya Mittal, IIT, New Deji, India
Wilma Olson, Rutgers Univ.
Anna Panchenko, NCBI, NLM, NIH
Wolfram Saenger, Free Univ. of berlin, Germany
Harold Scheraga, Cornell Univ.
Jiri Sponer, Institute of Biophysics, Czech Republic
Tom Tullius, Boston Univ.
Volodya Uversky, IUPUI
Sybren S. Wijmenga, Radboud Univ. Nijmegen, The Netherlands
Krystyna Zakrzewska, IBCP, France
Speakers, Chairs and Guests
Adams, Claire, Univ. of Kentucky
Aguilera, Jesus Javier, RPI
Anand, Swadha, NII, New Delhi
Artamonova, Irena, Vavilov Institute, Moscow, Russia
Avila-Figueroa, Amalia, Brown Univ.
Avvedimento, Vittorio Enrico, Univ. Federico II di Napoli, Italy
Azad, Robert; Boston Univ
Bahar, Ivet, Univ. of Pittsburgh
Bakan, Ahmet, Univ. of Pittsburgh
Banas, Pavel, Palacky Univ. Olumouc, Czech Republic
Barsegov, Valeri, Univ. of Mass, Lowell
Barvik, Ivan, Charles Univ., Czech Republic
Belotserkovskii, Boris, Stanford, Univ.
Berezovsky, Igor, Univ. of Bergen, Norway
Bernard, Sarah; Boston Univ.
Besseova, Ivana, Institute of Biophysics, Czech Republic
Beveridge, David, Wesleyan Univ.
Bhattacharyya, Moitrayee, IISc, Bangalore, India
Bichenkova, Elena, Univ. of Manchester, UK
Bishop, Tom, Tulane University
Bryce, Richard, Univ. of Manchester, UK
Bulyk, Martha, Harvard Medical School
Cantara, William, University at Albany
Castor, Katie, McGill Univ., Montreal, Canada
Chakrabarti, Pinak, Bose Institute, Calcutta, India
Chandrasekaran, Arun R, New York Univ.
Cheatham, Thomas, University of Utah
Cheguri, Srujana, RIT, Rochester
Chen, Jie, Columbia Univ.
Chen, C. Y. C., China Medical University, Taiwan
Chiang, Cheryl, Boston Univ.
Chong, Lillian T, Univ. of Pittsburgh
Cowburn, David, Albert Einstein College of Medicine
Cremer, Thomas, Univ. of Muenchen, Germany
Cui, Feng, NIH
Cunningham, Rick, SUNY at Albany
Dai, Ling, New York Univ.
Dang, Na Le, Wesleyan Univ.
Das, Payel, IBM
Dasgupta, Amrita, NCBS, Bangalore, India
Dastidar, Shubhra G., Bose Institute, Calcutta, India
Daughdrill, Gary, Univ. of Southern Florida
De Etoulem, Venise Rita, Brown Univ.
De Fabritiis, Gianni, Univ. Pompeu Fabra, Barcelona, Spain
DeFelice, James, RIT, Rochester
Delanney, Sarah, Brown Univ.
Dey, Raja, Univ. of Southern Calif.
Dias, James A, Vice President, Research, Univ. at Albany
Dill, Ken, UCSF
Dima, Ruxandra, Univ. of Cincinnati
Di Mauro, Ernesto, Univ. of Rome, Italy
Dror, Iris, Univ. of Southern California & Technion, Israel
Duax, William, Hauptman-Woodward Institute
Dupureur, Cynthia, Univ of Missouri St Louis
Endutkin, Anton, SB RAS ICB, Novosibirsk, Russia
Eliezer, David, Cornell
Fabris, Dan, SUNY at Albany
Fedorova, Olga, ICB, Novosibirsk, Russia
Ferris, James, RPI
Fojta, Miroslav Institute of Biophysics, Czech Republic
Frank-Kamenetskii, Maxim, Boston Univ.
Fried, Michael, Univ. of Kentucky
Froehlich, Chris, MDC-belin, Germany
Fudenberg, Geoffrey, Harvard
Gabrielian, Anna, RTCOPC, Yeravan, Armenia
Gao, Xiang, New York Univ.
Garcia, Angel, RPI
Gelfand, Mikhail, IITP, Moscow, Russia
Ghosh, Anirban, C-ADC, Pune, India
Ghosh, Saptaparni, Saha Institute, Calcutta, India
Gomez-Alcala, Pilar, Columbia Univ.
Gothelf, Kurt Vesterager, Aarhus Univ., Denmark
Gur, Mert, Univ. of Pittsburgh
Hagan, William, College of St Rose
Hakker, Lauren, Univ. at Albany
Hammond, Nicholas, Boston Univ.
Hannestad, Jonas, Chalmers Univ., Göteborg, Sweden
Haran, Tali, Technion, Israel
Harish, Balasubramaniam, Princeton Univ.
Harris, Kimberly, Univesity at Albany
Harris, Lydia-Ann, Univ. at Buffalo
Harris, Reuben, Univ. of Minnesota
Hashimoto, Kosuke, NIH
Heinemann, Udo, MDC, Berlin, Germany
Hernandez, Carina, New York Univ.
Hingorani, Manju, Wesleyan Univ.
Holcomb, Dana, Boston Univ.
Honig, Barry, Columbia Univ.
Horovitz, Amnon, Weizmann Institute, Israel
Huang, Ji, Brown University
Hud, Nick, Georgia Tech
Ingle, Shakti, Boston Univ.
Isin, Basak, Univ of Pittsburgh
Ivanov, Alexander, ICBCR, Moscow, Russia
Jain, Swapan, Bard College
Jani, Vinod, C-ADC, Pune, India
Jarem, Daniel, Brown Univ.
Jatana, Nidhi, Sri Venkateswara Col., Delhi, India
Jayaram, B., IIT, New Delhi, India
Jeruzalmi, David, Harvard
Ji, Liangnian, Sun Yat-Sen Univ., Guanghhou, China
Jinks-Robertson, Sue, Duke Univ.
Joshi, Prakash, RPI
Kallenbach, Neville, NYU
Kel, Alexander, GeneXplain GmbH, Germany
Kolkman, Ard, Radboud Univ. Nijmegen, The Netherlands
Kolpashchikov, Dmitry, Univ. of Central Florida
Kotzer, Uri, New York Univ.
Koudelka, Gerald, Univ. at Buffalo.
Kovalenko, Ilya, Moscow State Univ., Russia
Kravats, Andrea, Univ. of Cincinnati
Kulakovskiy, Ivan, EIMB, RAS, Moscow, Russia
Lazarovici, Allan, Columbia Univ.
Levy, Koby, Weizmann Institute, Israel
Lee, Rebecca, Wesleyan Univ.
Li, Dadong, New York Univ.
Li, Duan, Univ. of Cincinnati
Li, Yuhang, New York Univ.
Liu, Jingyuan, IUPUI
Liu, Peng, Columbia Univ.
Liu, Wenyan, New York Univ.
Lomzov, Alexander, ICB, Novosibirsk, Russia
Lukin, Mark, SUNY at Stony Brook
Lundberg, Erik, Chalmers Univ., Göteborg, Sweden
Maciejczyk, Maciej, Univ. of Warmia and Mazury, Poland
Maeshima, Kazuhiro, NIG, Mishima, Japan
Makeev, Vsevolod, GosNIIGenetika, Moscow, Russia
Marky, Luis, Univ. of Nebraska Med. Center
Martadinata, Herry, NTU, Singapore
McFarland, Christopher, Harvard Univ.
Mamajanov, Irena, Georgia Tech
Mann, Richard, Columbia Univ.
Marx, Kenneth, Univ. of Mass., Lowell
Mauricio, Esguerra, Karolinska Institutet, Sweden
Mayr, Florian, MDC-Berlin, Germany
Meierhenrich, Uwe, Univ. of Nice-Sophia Antipolis, France
Menaria, Khushhali, MANIT, Bhopal, India
Mezei, Mihaly, Mount Sinai
Michel, Benedicte, CNRS, Gif-sur-Yvette, France
Mirkin, Sergei, Tufts Univ.
Mittal, Aditya, IIT, New Delhi, India
Morgunov, Igor, Skryabin IBPM, Pushchino, Russia
Mueller, Christoph, EMBL, Heidelberg, Germany
Mukerji, Ishita, Wesleyan Univ.
Mukherjee, Goutam, IIT Delhi, India
Mukherjee, Rajib, Tulane Univ.
Nguyen, Khiem, Univ. of Utah
Nguyen, Nam, New York Univ.
Nielsen, Peter, Univ. of Copenhagen, Denmark
Niu, Dong, New York Univ.
Norden, Bengt, Chalmers Univ, Sweden
O’Donnell, Mike, Rockefeller Univ.
Ohayon, Yoel, New York Univ.
Olson, Wilma, Rutgers Univ.
Oskan, Sefica Banu, Arizona Sate Univ., Tempe, AZ
Otyepka, Michal, Palacky Univ. Olumouc, Czech Republic
Ozoline, Olga, RAS, Pushchino, Russia
Panchenko, Anna, NCBI, NLM, NIH
Perez, Alberto, Stony Brook Univ.
Perez, Juan-Jesus, Univ. of Catalonia, Spain
Parker, Steve, NIH
Petrov, Valery, IBPM, Pushchino, Russia
Pieniazek, Susan, Wesleyan Univ.
Pirchi, Menahem, Weizmann, Israel
Pogenberg, Vivian, EMBL, Hamburg, Germany
Priya, Preety, RIT, Rochester
Racca, Joe, Casewestern Reserv Univ.
Reblova, Kamila, Institute of Biophysics, Czech Republic
Reymer, Anna, Chalmers Univ, Sweden
Rich, Alex, MIT
Riley, Todd, Columbia Univ.
Ritschoff, Claire, Boston Univ
Rohs, Remo, Univ. of Southern California
Rozenberg, Hiam, Weizmann, Israel
Ruben, George, Dartmouth
Saenger, Wolfram, Free Univ. of Berlin, Germany
Sagi, Irit, Weizmann Institute, Israel
Samchenko, Alexander, ICB, Pushchino, Russia
Scheraga, Harold, Cornell Univ.
Schulten, Klaus, Univ. of Illinois
Schvartzman, Jorge Bernardo, CSIC, Madrid, Spain
Seeman, Ned, NYU
Sha, Ruojie, New York Univ.
Shakked, Zippi, Weizmann, Israel
Sharma, Anushi, Wesleyan Univ.
Shrivastava, Indirani, Univ. of Pittsburgh
Singh, Sanjeev, Alagappa Univ., Karaikudi, India
Simmel, Friedrich, Technische Univ. München, Germany
Slattery, Matthew, Univ. of Chicago
Sonavane, Uddhav, CDAC, Pune, India
Sorokin, Anatoly, ICBRAS, Pushcino, Moscow, Russia
Sponer, Jiri, Institute of Biophysics, Czech Republic
Srinivasan, Saipraveen, RPI
Stan, George, Univ. of Cicinnati
Subramanian, Hari, K. K., NYU and Boston Univ.
Szostak, Jack, Harvard Medical School, Nobel Laureate
Tainer, John, Scripps
Takashima, Akihiko, RIKEN, Japan
Thirumalai, Dave, Univ. of Maryland
Tolbert, Blanton, Miami Univ., Oxford, OH
Tonddast-Navaei, Sam, Univ. of Cincinnati
Traaseth, Nate, NYU
Trifonov, Edward, Univ. of Haifa, Israel
Tullius, Tom, Boston Univ.
Udomprasert, Anuttara, New York Univ.
Ulyanov, Nick, UCSF
Volle, Catherine, Brown Univ.
Vorobyev, Yury, ICB, Novosibirsk, Russia
Wang, Jihua, Dezhou Univ., Dezhou, China
Wheatley, Elizabeth, Wesleyan Univ.
Widom, Jonathan, Northwestern Univ.
Wijmenga, Sybren, Radboud Univ. Nijmegen, The Netherlands
Wilhelmsson, Marcus, Chalmers Univ., Göteborg, Sweden
Williams, Loren, Georgia Tech
Yang, Huiying, Sun Yat-Sen Univ., Guanghhou, China
Ye, Miao, New York Univ.
Yennie, Craig, Brown Univ
Wolfe, Scot, Univ. of Mass. Medical School
Young, Matthew, Univ. of Michigan Ann Arbor
Zakrzewska, Krystyna, IBCP, France
Zharkov, Dmitry, SB RAS ICB, Novosibirsk, Russia
Zhao, Xinshuai, New York Univ.
Zhou, Tianyin, Univ. of Southern California
Zhou, Yayan, Wesleyan Univ.
Zhmurov, Artem, Univ of Mass Lowell
Zhurkin, Victor, NIH
Zomot, Elia, Univ. of Pittsburgh