Academic Profile

Academic Profile

Assoc Prof Konstantin Pervushin

Associate Professor, School of Biological Sciences

Email: kpervushin@ntu.edu.sg
Assoc Prof Konstantin Pervushin

Biography
1991-1994 PhD program at the Institute of Bioorganic Chemistry in Moscow
1994-1997 Postdoctoral training an the Institut für Molekularbiologie und Biophysik, ETH-Zürich, Supervision Prof. Kurt Wüthrich.
1997 Seniour Researcher at the ETH Zürich, laboratory of Prof. Kurt Wüthrich.
2000 Assistant Professor, Laboratorium für Physikalische Chemie, ETH Zurich.
2006.10 Associate Professor, School of Biological Sciences, NTU, Singapore
Research Interests
Solution NMR spectroscopy. NMR in solution will be used as a primary tool to elucidate structure and dynamics of IAPP and its mimics in physiologically relevant complexes encountered in health. I specialize on NMR pulse sequence, software and hardware developments in the area of NMR spectroscopy of biomolecules in solution using NMR. The main focus is development of advanced solution NMR and computational techniques to attack challenging biological problems such as structure/dynamics investigations of refolded proteins, membrane proteins, structures of molecular machines assisting heme transfer and folding of other proteins, ligand/protein complexes, large multimeric enzymes, ion channels. We developed a new TROSY concept, which allowed structural studies of large proteins (e.g. 220 kDa complex of immuno-complement proteins). Since NMR structural work should be conducted with medium and large (according to current NMR standards) proteins and protein complexes the use of the advanced NMR techniques such as TROSY, CRINEPT, LTROSY and TROSY-SPI will be critical. Dynamic behaviour of IAPP and analogues will be studied by NMR relaxation methods developed. We developed an automatic assignment of protein resonances program SideLink and extended it to direct spectrum analysis drastically speeding up structure determination of medium sized proteins.
Current Projects
  • Bioinspired Coacervation for Green Processing of Biomolecular Composites
  • Comparative studies of the structure and adhesion properties of the aLB2, aMb2, aXb2 integrin, and the crystallographic studies of the b2 and b3 integrin
  • Discovering inhibitors against the Dengue virus NS3 helicase and NS5 polymerase using a fragment-based approach aided by X-ray crystallography, N.M.R. and Surface Plasmon resonance
  • Explore the Intrinsic Disordered Nature of Structures of Human Islet Amyloid Polypeptide and Its Amyloid Formation Mechanism By Combined Computational and Nuclear Magnetic Resonance Study
  • Hybrid high resolution structure determination of helical filaments using cryo-EM and solid state NMR spectroscopy
  • Improving feedback on short essays in biology courses through an AI-aided assessment
  • Mechanism of chaperone function of prostaglandin synthase for amyloid b-peptides
  • Molecular mechanisms of Barnacle Adhesion: A Combined Structural Biology and Computational Study
  • NMR Structural Characterization Of TGFBI Protein And AmyloidFibrils In Corneal Dystrophies
  • NMR Structures of Synthetic Xanthones and Their Bactericidal Mechanism Studies by NMR
  • NMR structural studies of beta-catenin/BCL9 interactions as a potential drug target in colorectal cancer
  • Solid-state NMR study of heterochromatin maintenance by HP1 protein at telomeres
  • Structural basis of amyloid seeds disaggregation by neuroprotective chaperones as a novel therapeutic avenue in TGFBIp-related corneal dystrophies
  • Structural basis of hydrolysis of RNA catalyzed by GCN4 leucine zipper
  • Structural response of chromatin to epigenetic modifications by solid state NMR
  • The protein chemistry of integrin adhesion molecules
  • Towards Understanding of Eukaryotic Translation Termination : NMR Structural Studies of Human Peptide Release Factor eRF1 and Its Interactions With Ribosomal Pre-Termination Complex By NMR In Solution
Selected Publications
  • Wei L, Jiang P, Manimekalai MSS, Hunke C, Gruber G, Pervushin K, Mu Y. (2015). Extended structure of rat islet amyloid polypeptide in solution. Advances in Experimental Medicine and Biology, 827, 85-92.
  • Lim SM, Chen D, Teo H, Roos A , Jansson AE, Nyman T , Trésaugues L , Pervushin K, Nordlund P. (2013). Structural and dynamic insights into substrate binding and catalysis of human lipocalin Prostaglandin D synthase. Journal of Lipid Research, 54(6), 1630-43.
  • Tan E, Rao F, Pasunooti S, Pham TH, Soehano I, Turner MS, Liew CW, Lescar J, Pervushin K and Liang Z-X. (2013). Solution Structure of the PAS Domain of a Thermophilic YybT Homolog Reveals a Potential Ligand-Binding Site. Journal of Biological Chemistry, 288(17), 11949-11959.
  • How, Jonathan; Zhang, Ai; Phillips, Margaret; Reynaud, Aline; Lu, Si Yan; Pan, Lucy Xin; Ho, Hai Ting; Yau, Yin Hoe; Guskov, Albert; Pervushin, Konstantin; Shochat, Susana Geifman; Eshaghi, Said; Koch, Karl-Wilhelm. (2013). Comprehensive Analysis and Identification of the Human STIM1 Domains for Structural and Functional Studies. PLoS ONE, 8(1), e53979-.
  • Li, J., S. Liu, R. Lakshminarayanan, Y. Bai, K. Pervushin, C. Verma, and R. W. Beuerman. (2013). Molecular simulations suggest how a branched antimicrobial peptide perturbs a bacterial membrane and enhances permeability. Biochimica et Biophysica Acta, 1828(3), 1112-21.

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