Day 1 :
Keynote: Title: RASER (Rate Amplification based on the Substrate-Enhanced Reaction) Model of Single-Molecule Enzyme Catalysis
Time : 09:50-10:50
Sungchul Ji has completed his PhD from State Univeristy of New York at Albany and Post-doctoral studies from University of Wisoconsin in Madison, University of Pennsylvaniac School of Medicine, Max Planck Institute of Systems Physiology in Dortmund, and University of North Carolina School of Medicine at Chapel Hill, before joining the Faculty of the Rutgers University Ernest Mario School of Pharmacy in Piscataway, N.J. He has published two books on the Molecular Theories of the Living Cell (Springer, 2012) and the Cell Language Theory (World Scientific, 2017) and about 50 papers in reputed journals.
Single-molecule enzyme turnover times produce long-tailed histograms fitting the Planckian Distribution Equation (PDE), a generalized version of the blackbody radiation equation. RASER is the acronym derived from rate amplification based on the substrate-enhanced reaction, in analogy to laser (Light Amplification based on Stimulated Emission of Radiation). Just as the blackbody radiation equation of Planck, when generalized to PDE, was found to apply to single-molecule enzyme catalysis, so may the subatomic mechanisms of laser as here proposed. The quantization of the Gibbs free energy content of enzymes was inferred from the fitting of the single-molecule-molecule turnover-time histogram of cholesterol oxidase to PDE. When an enzyme molecule absorbs enough thermal energies through Brownian motions, it may be excited to the transition state from which the enzyme may be demoted back to one of its ground states in two ways – (i) spontaneously (as in “spontaneous emission” in laser), or (ii) induced by substrate binding (as in “induced emission”). During the substrate-induced deactivation of the excited enzyme, the excess energy may be released in a coordinated manner effectuating catalysis, just as the triggering photon-induced de-activation of population-inverted electrons in atoms results in the amplification of emitted photons as laser. The RASER model of enzyme catalysis thus embodies two of the most fundamental processes in physics, i.e., (i) energy quantization, and (ii) the light amplification via laser.
Head of Proteomics Lab
Time : 11:10-12:10
Stanislav Naryzhny obtained his PhD from the Biophysics Institute in Pushchino, Russia and did his Postdoctoral Studies from St. Petersburg Nuclear Physics Institute (PNPI), Gatchina, Russia and from the Northeastern Ontario Regional Cancer Centre, Sudbury, Canada. He is the Head of Proteomics Laboratory of Petersburg Nuclear Physics Institute at National Research Center "Kurchatov Institute" and also Chief Scientist at Institute of Biomedical Chemistry, Moscow, Russia. He is a protein Biochemist with extensive hands-on experience in academia with strong background in protein structure-function theory and expertise in processes involved in DNA replication, DNA stability and tumorigenesis; protein, protein structure and proteomics analysis employing a wide variety of biophysical and biochemical methods. His area of research lies in the two-dimensional gel electrophoresis (2DE) based proteomics, where he has published more than 40 papers in reputed journals.
Human proteome is tremendously complex and composed from diverse and heterogeneous gene products (proteoforms). Recent developments in mass spectrometry and systematic approaches (technology and methodology) promise to bring new insights into this complexity. A combination of mass spectrometry with classical biochemical separation technologies is particularly attractive for this systematic investigation. Among biochemical methods, two-dimensional gel electrophoresis (2DE) is a most powerful protein separation technique that allows not just separating proteoforms but determining their physic-chemical parameters (pI and Mw). In our study, we performed the panoramic analysis of cellular proteins using a combination of virtual (in silico) and experimental 2DE with high-resolution nano-liquid chromatography-mass spectrometry. This approach is moving proteomics study on the next level of the acquisition of knowledge about proteomes. To get better impression about diversity of proteoforms in a particular proteome, whole gels (not just spots but sections) were analyzed using this approach. This allowed to detecting in a single proteome more than 20000 proteoforms coded by more than 4000 genes. The 3D-graphs showing distribution of these proteoforms including proteoforms of biomarkers in 2DE map were generated. A comparative analysis of these graphs between normal and cancer cells was performed. This analysis showed a high variability and dynamics of proteoforms.