S. Samar Hasnain

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S. Samar Hasnain FInstP, FRSC, is the inaugural Max Perutz professor of Molecular Biophysics at the University of Liverpool. In 1991 he became a Fellow of the Institute of Physics and in 2002 he became a Fellow of the Royal Society of Chemistry. In 1997 he became a Fellow of the Third World Academy of Sciences. He became Foreign Fellows of Pakistan Academy of Sciences in 2017.[1]

Education[edit]

In 1970 Hasnain earned a Bachelor of Science (Honours) an M.Sc. in 1972 from the University of Karachi and a Ph.D. in 1976 from the University of Manchester on Molecular Crystals, using synchrotron radiation from the NINA facility.

Career and Research[edit]

After spending a year as Post-Doctoral Research Associate at Manchester he joined DESY in Hamburg as a DESY Fellow working on the Storage ring Synchrotron Radiation Facility, where the synchrotron team created HASYLAB in 1978.

In 1979, Professor Hasnain joined the Daresbury Laboratory as a member of the team establishing the world’s first dedicated X-Ray synchrotron radiation source (the SRS). In 1989, he established the Molecular Biophysics group at Daresbury, where he remained as head of the group until March 2008 when he moved to the University of Liverpool. During 2011-2105 he was the International Lead for the Faculty of Health and Life Sciences of the university.

In 1982, Hasnain helped Perutz to resolve a controversy in the mechanism of oxygen uptake by haemoglobin.[2][3][4]

He is the founding Editor of the International Union of Crystallography’s (IUCr) Journal of Synchrotron Radiation in 1993 and was Editor in Chief of IUCr Journals from 2012 to 2018. In 2014, he launched the IUCr’s flagship journal IUCrJ. He is a member of the International Advisory Board for IUCrJ. He is also an Editor of the journal Current opinion in Structural Biology.

He has been engaged with the SESAME synchrotron project in Jordan, launched under the umbrella of UNESCO, since its inception in 2004 and has been the UK Government’s representative on its council since its foundation. He has been chair of its Programme Review committee since 2018.[5]

His main research interest is in structure-function studies of proteins and their complexes that are involved in biological electron transfer,[6] nitrogen cycles[7][8][9][10][11] and neurodegenerative diseases[12][13][14][15][16][17][18][19] and in structure-based drug discovery targeted towards neurodegenerative diseases and malaria.

Hasnain has pioneered an approach to defining the structures of metalloproteins that combines not only X-ray crystallography[20] and solution X-ray scattering,[21] now used widely in the structural biology community, but also X-ray absorption fine structure (XAFS)[22][23][24][25] and optical spectroscopies. More recently, he has used cryo-electron microscopy (cryo-EM), applied to a number of membrane proteins. The integration of spectroscopic methods with crystallography and the use of XFEL radiation for providing damage-free structures for redox proteins.[26]

In 2019, Hasnain and Prof. Richard Catlow co-authored an article[27] giving personal accounts of how their work in the fields of structural molecular biology, materials and catalytic science developed and evolved using synchrotron techniques.

References[edit]

  1. ^ "Pakistan Academy of Sciences | Fellow Profile".
  2. ^ Perutz, M. F.; Hasnain, S. Samar; Duke, P. J.; Sessler, J. L.; Hahn, J. E. (1982). "Stereochemistry of iron in deoxyhaemoglobin". Nature. 295 (5849): 535–538. Bibcode:1982Natur.295..535P. doi:10.1038/295535a0. PMID 7057913. S2CID 4309029.
  3. ^ Science is Not a Quiet Life, Max Perutz, 1998, ISBN 978-981-02-2774-6 (hardcover), ISBN 978-981-02-3057-9 (softcover), ISBN 978-981-4498-51-7 (ebook)
  4. ^ Architects of Structural Biology: Bragg, Perutz, Kendrew, Hodgkin, John Meurig Thomas, 2020, ISBN 978-0-19-885450-0.
  5. ^ "Samar Hasnain – UNESCO in the UK". Retrieved 2020-08-04.
  6. ^ Antonyuk, Svetlana V.; Han, Cong; Eady, Robert R.; Hasnain, S. Samar (2013). "Structures of protein–protein complexes involved in electron transfer". Nature. 496 (7443): 123–126. Bibcode:2013Natur.496..123A. doi:10.1038/nature11996. PMC 3672994. PMID 23535590.
  7. ^ Leferink, Nicole G. H.; Antonyuk, Svetlana V.; Houwman, Joseline A.; Scrutton, Nigel S.; Eady, Robert R.; Hasnain, S. Samar (2014). "Impact of residues remote from the catalytic centre on enzyme catalysis of copper nitrite reductase". Nature Communications. 5: 4395. Bibcode:2014NatCo...5.4395L. doi:10.1038/ncomms5395. PMC 4104443. PMID 25022223.
  8. ^ Antonyuk, Svetlana V.; Strange, Richard W.; Sawers, Gary; Eady, Robert R.; Hasnain, S. Samar (2005). "Atomic resolution structures of resting-state, substrate- and product-complexed Cu-nitrite reductase provide insight into catalytic mechanism". Proceedings of the National Academy of Sciences. 102 (34): 12041–12046. Bibcode:2005PNAS..10212041A. doi:10.1073/pnas.0504207102. PMC 1189323. PMID 16093314.
  9. ^ Dodd, Fraser E.; Van Beeumen, Jos; Eady, Robert R.; Hasnain, S.Samar (1998). "X-ray structure of a blue-copper nitrite reductase in two crystal forms. The nature of the copper sites, mode of substrate binding and recognition by redox partner 1 1Edited by R. Huber". Journal of Molecular Biology. 282 (2): 369–382. doi:10.1006/jmbi.1998.2007. PMID 9735294.
  10. ^ Strange, Richard W.; Dodd, Fraser E.; Abraham, Zelda H.L.; Grossmann, J. Günter; Brüser, Thomas; Eady, Robert R.; Smith, Barry E.; Hasnain, S. Samar (1995). "The substrate-binding site in Cu nitrite reductase and its similarity to Zn carbonic anhydrase". Nature Structural & Molecular Biology. 2 (4): 287–292. doi:10.1038/nsb0495-287. PMID 7796265. S2CID 21986822.
  11. ^ Vanadium K-edge X-ray absorption spectrum of the VFe protein of the vanadium nitrogenase of Azotobacter chroococcum  [(1987) Arber, J. M., Dobson, B. R., Eady, R. R., Stevens, P., Hasnain, S. S., Garner C. D. and Smith, B. E.
  12. ^ Capper, Michael J.; Wright, Gareth S. A.; Barbieri, Letizia; Luchinat, Enrico; Mercatelli, Eleonora; McAlary, Luke; Yerbury, Justin J.; o'Neill, Paul M.; Antonyuk, Svetlana V.; Banci, Lucia; Hasnain, S. Samar (2018). "The cysteine-reactive small molecule ebselen facilitates effective SOD1 maturation". Nature Communications. 9 (1): 1693. Bibcode:2018NatCo...9.1693C. doi:10.1038/s41467-018-04114-x. PMC 5923229. PMID 29703933.
  13. ^ Wright, Gareth S.A.; Antonyuk, Svetlana V.; Kershaw, Neil M.; Strange, Richard W.; Samar Hasnain, S. (2013). "Ligand binding and aggregation of pathogenic SOD1". Nature Communications. 4: 1758. Bibcode:2013NatCo...4.1758W. doi:10.1038/ncomms2750. PMC 3644087. PMID 23612299.
  14. ^ Hough, Michael A.; Grossmann, J. Günter; Antonyuk, Svetlana V.; Strange, Richard W.; Doucette, Peter A.; Rodriguez, Jorge A.; Whitson, Lisa J.; Hart, P. John; Hayward, Lawrence J.; Valentine, Joan Selverstone; Hasnain, S. Samar (2004). "Dimer destabilization in superoxide dismutase may result in disease-causing properties: Structures of motor neuron disease mutants". Proceedings of the National Academy of Sciences. 101 (16): 5976–5981. doi:10.1073/pnas.0305143101. PMC 395908. PMID 15056757.
  15. ^ Elam, Jennifer Stine; Taylor, Alexander B.; Strange, Richard; Antonyuk, Svetlana; Doucette, Peter A.; Rodriguez, Jorge A.; Hasnain, S Samar; Hayward, Lawrence J.; Valentine, Joan Selverstone; Yeates, Todd O.; Hart, P John (2003). "Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS". Nature Structural & Molecular Biology. 10 (6): 461–467. doi:10.1038/nsb935. PMID 12754496. S2CID 22507679.
  16. ^ Strange, Richard W.; Antonyuk, Svetlana; Hough, Michael A.; Doucette, Peter A.; Rodriguez, Jorge A.; Hart, P.John; Hayward, Lawrence J.; Valentine, Joan S.; Hasnain, S.Samar (2003). "The Structure of Holo and Metal-deficient Wild-type Human Cu, Zn Superoxide Dismutase and its Relevance to Familial Amyotrophic Lateral Sclerosis". Journal of Molecular Biology. 328 (4): 877–891. doi:10.1016/S0022-2836(03)00355-3. PMID 12729761.
  17. ^ Antonyuk, S. V.; Trevitt, C. R.; Strange, R. W.; Jackson, G. S.; Sangar, D.; Batchelor, M.; Cooper, S.; Fraser, C.; Jones, S.; Georgiou, T.; Khalili-Shirazi, A.; Clarke, A. R.; Hasnain, S. S.; Collinge, J. (2009). "Crystal structure of human prion protein bound to a therapeutic antibody". Proceedings of the National Academy of Sciences. 106 (8): 2554–2558. Bibcode:2009PNAS..106.2554A. doi:10.1073/pnas.0809170106. PMC 2637903. PMID 19204296.
  18. ^ Samantha, Price (4 March 2014). "TDP-43: A protein that lingers on." (Web page). Proceedings of the National Academy of Sciences of the United States of America. 111 (11). Motor Neurone Disease Association: 4309–14. Bibcode:2014PNAS..111.4309A. doi:10.1073/pnas.1317317111. PMC 3964094. PMID 24591609. Retrieved 30 April 2014.
  19. ^ Austin, J. A.; Wright, G. S. A.; Watanabe, S.; Grossmann, J. G.; Antonyuk, S. V.; Yamanaka, K.; Hasnain, S. S. (2014). "Disease causing mutants of TDP-43 nucleic acid binding domains are resistant to aggregation and have increased stability and half-life". Proceedings of the National Academy of Sciences. 111 (11): 4309–14. Bibcode:2014PNAS..111.4309A. doi:10.1073/pnas.1317317111. PMC 3964094. PMID 24591609.
  20. ^ Bailey, Susan; Evans, Robert W.; Garratt, Richard C.; Gorinsky, Beatrice; Hasnain, Samar; Horsburgh, Christopher; Jhoti, Harren; Lindley, Peter F.; Mydin, Assanah; Sarra, R. (1988). "Molecular structure of serum transferrin at 3.3-.ANG. Resolution". Biochemistry. 27 (15): 5804–5812. doi:10.1021/bi00415a061. PMID 3179277.
  21. ^ Grossmann, J.Günter; Neu, Margarete; Pantos, Emmanuel; Schwab, Franz J.; Evans, Robert W.; Townes-Andrews, Elizabeth; Lindley, Peter F.; Appel, Helmut; Thies, Wolf-Gerolf; Hasnain, S.Samar (1992). "X-ray solution scattering reveals conformational changes upon iron uptake in lactoferrin, serum and ovo-transferrins". Journal of Molecular Biology. 225 (3): 811–819. doi:10.1016/0022-2836(92)90402-6. PMID 1602483.
  22. ^ Binsted, Norman; Strange, Richard W.; Hasnain, S. Samar (1992). "Constrained and restrained refinement in EXAFS data analysis with curved wave theory". Biochemistry. 31 (48): 12117–12125. doi:10.1021/bi00163a021. PMID 1280998. S2CID 45063154.
  23. ^ Arber, J. M.; De Boer, E.; Garner, C. D.; Hasnain, S. S.; Wever, R. (1989). "Vanadium K-edge x-ray absorption spectroscopy of bromoperoxidase from Ascophyllum nodosum". Biochemistry. 28 (19): 7968–7973. doi:10.1021/bi00445a062. PMID 2611224.
  24. ^ The CO bond angle of carboxymyoglobin determined by angular resolved XANES spectroscopy (1985) Bianconi, A., Congiu-Castellano, A., Durham, P. J., Hasnain S. S. and Phillips, S., Nature, 318, 685-687.
  25. ^ Hasnain, S.Samar; Murphy, Loretta M.; Strange, Richard W.; Grossmann, J.Günter; Clarke, Anthony R.; Jackson, Graham S.; Collinge, John (2001). "XAFS study of the high-affinity copper-binding site of human PRP 91–231 and its low-resolution structure in solution 1 1Edited by I. A. Wilson". Journal of Molecular Biology. 311 (3): 467–473. doi:10.1006/jmbi.2001.4795. PMID 11493001.
  26. ^ Halsted, Thomas P.; Yamashita, Keitaro; Hirata, Kunio; Ago, Hideo; Ueno, Go; Tosha, Takehiko; Eady, Robert R.; Antonyuk, Svetlana V.; Yamamoto, Masaki; Hasnain, S. Samar (2018). "An unprecedented dioxygen species revealed by serial femtosecond rotation crystallography in copper nitrite reductase". IUCrJ. 5 (Pt 1): 22–31. doi:10.1107/S2052252517016128. PMC 5755574. PMID 29354268.
  27. ^ Hasnain, S. Samar; Catlow, C. Richard A. (2019). "Synchrotron science in the UK: NINA, the SRS and Diamond". Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences. 377 (2147). Bibcode:2019RSPTA.37790147H. doi:10.1098/rsta.2019.0147. PMC 6501895. PMID 31030660.
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