个人简介

Nozomi received her graduate and postdoctoral training in the labs of Sol Gruner and Cathy Drennan, where she developed a love of synchrotrons and enzymes (metalloenzymes in particular). She enjoys the spaceship-like feel of synchrotrons and has been on about 30 trips, of which 26 were for small-angle X-ray scattering (SAXS) studies. Apart from science, she enjoys classical singing. She looks forward to working with students and postdocs from diverse backgrounds.

研究领域

Protein structural dynamics/structural enzymology/X-ray physics.

What are the structural dynamics involved in protein allostery and catalysis? How do flexible enzymes perform challenging chemistry? Can we animate crystal structures of proteins? These are outstanding questions in biology, which motivate studies of proteins in motion. Capturing molecular movies of proteins in action is the next frontier of structural enzymology. Towards this goal, our group will develop advanced X-ray based methods, such as time-resolved X-ray scattering, in order to examine the role of structural dynamics in enzyme function at multiple length- and timescales. Enzymes that utilize metal-containing cofactors (i.e. metalloenzymes) are of particular interest to our research, both for the fascinating reactions that they are able to catalyze and for their physical properties. In addition to performing biochemical and biophysical characterizations in-house, our group will design and fabricate devices and heavily utilize synchrotron X-rays.

近期论文

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S Skou, RE Gillilan, N Ando*. “Synchrotron-based small-angle X-ray scattering (SAXS) of biomacromolecules in solution.” Nature Protocols (2014), 9: 1727–1739. *corresponding. EC Minnihan, N Ando*, EJ Brignole*, L Olshansky*, J Chittuluru, FJ Asturias, CL Drennan, DG Nocera, and J Stubbe. “Generation of a stable, aminotyrosyl radical-induced α2β2 complex of Escherichia coli class Ia ribonucleotide reductase,” PNAS (2013), 110: 3835-3840. N Ando, Y Kung, M Can, G Bender, SW Ragsdale, CL Drennan. “Transient B12-dependent methyltransferase complexes revealed by small-angle X-ray scattering.” JACS (2012) 134: 17945–17954. CM Zimanyi, N Ando, EJ Brignole, FJ Asturias, J Stubbe, CL Drennan. “Tangled up in knots: Structures of inactivated forms of E. coli class Ia ribonucelotide reductase.” Structure (2012) 20: 1374–1383. S Wang, Y Meng, N Ando, MW Tate, S Krasnicki, C Yan, Q Liang, J Lai, H Mao, SM Gruner and RJ Hemley. “Single-crystal CVD diamonds as small-angle X-ray scattering windows for high-pressure research.” Journal of Applied Crystallography (2012) 45: 1–5. Y Kung, N Ando, T Doukov, L Blasiak, G Bender, SW Ragsdale, CL Drennan. “Visualizing molecular juggling within a B12-dependent methyltransferase complex.” Nature (2012) 484: 265–269. KD Bewley, MA Firer-Sherwood, J-Y Mock, N Ando, CL Drennan and SJ Elliott. “Mind the Gap: Diversity and reactivity relationships among multiheme cytochromes of the MtrA/DmsE family.” Biochemical Society Transactions (2012), 40: 1268–1273. EJ Brignole*, N Ando, CM Zimanyi, CL Drennan. “The prototypic class Ia ribonucleotide reductase from Escherichia coli: Still surprising after all these years.” Biochemical Society Transactions (2012) 40: 523–530. *equal contributions N Ando and B Barstow*. “High hydrostatic pressure effects on proteins: Fluorescence studies.” Encyclopedia of Analytical Chemistry, eds R.A. Meyers, John Wiley: Chichester. DOI: 10.1002/9780470027318.a9246. *co-corresponding, invited N Ando*, EJ Brignole*, CM Zimanyi, MA Funk, K Yokoyama, FJ Asturias, J Stubbe, CL Drennan. “Structural interconversions modulate activity of Escherichia coli ribonucleotide reductase.” PNAS (2011) 108: 21046–21051. *equal contributions MA Firer-Sherwood*, N Ando*, SJ Elliott, CL Drennan. “Solution-based structural analysis of the decaheme cytochrome, MtrA, by small angle X-Ray scattering and analytical ultracentrifugation.” J. Phys. Chem. B (2011) 115: 11208–11214. *equal contributions B Barstow, N Ando, CU Kim, SM Gruner. “Coupling of pressure-induced structural shifts to spectral changes in a Yellow Fluorescent Protein.”Biophysical Journal (2009) 97: 1719-1727. N Ando, B Barstow, WA Baase, A Field, BW Matthews, Sol M. Gruner. “Structural and thermodynamic characterization of T4 lysozyme mutants and the contribution of internal cavities to pressure denaturation.” Biochemistry (2008) 47: 11097-11109. B Barstow, N Ando, CU Kim, SM Gruner. “Alteration of Citrine structure by hydrostatic pressure explains accompanying spectral shift.” PNAS(2008) 105: 13362-13366. N Ando, P Chenevier, M Novak, MW Tate, SM Gruner. “High hydrostatic pressure small-angle X-ray scattering cell for protein solution studies featuring diamond windows and disposable sample cells.” Journal of Applied Crystallography (2008) 41: 167-175. A Batra, C Cohen; H Kim, KI Winey; N Ando, SM Gruner. “Counterion effect on the rheology and morphology of tailored poly(dimethylsiloxane) ionomers.” Macromolecules (2006) 39: 1630-1638. A Polozova, X Lia, T Shangguana, P Meersa, DR Schuette, N Ando, SM Gruner, WR Perkins. “Formation of homogeneous unilamellar liposomes from an interdigitated matrix.” Biochimica et Biophysica Acta (2005) 1668: 117–125. K Ito, J Chuang, C Alvarez-Lorenzo, T Watanabe, N Ando, and AY Grosberg. “Multiple contact adsorption of target molecules by heteropolymer gels.” Macromolecular Symposia (2004) 207: 1. K Ito, J Chuang, C Alvarez-Lorenzo, T Watanabe, N Ando and AY Grosberg. “Multiple point adsorption in a heteropolymer gel and the Tanaka approach to imprinting: experiment and theory.” Progress in Polymer Science (2003) 28: 1489-1515.