Michael C. Wiener

Education

  • BS, University of Rochester
  • PhD, Carnegie Mellon University
  • Postdoc, University of California, Irvine
  • Postdoc, University of California, San Francisco

Primary Appointment

  • Professor, Molecular Physiology and Biological Physics

Contact

Research Interest(s)

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Research Description

http://abnehmenmitspass.info/?v=insurance-coverage-for-viagra insurance coverage for viagra The structure/function paradigm is of central import in modern molecular biology. High-resolution structures, determined by x-ray crystallography, of proteins involved in biological processes provide insight into their function. These structures provide a basis for the design of future experiments to probe more deeply the precise molecular mechanisms that underlie biological activity. In addition to providing fundamental insight into function and mechanism, structures of proteins involved in disease and other pathophysiological states can serve as targets for structure-based drug design. We propose a structure-based approach to the determination of membrane protein function. Our goal is to solve x-ray crystal structures of channel, transport and receptor proteins, and to use these structures in conjunction with other results to understand the molecular basis of function. While thousands of soluble protein structures have been solved (at a rate of about three per day!), very few integral membrane proteins have been solved to high resolution. Major technical, scientific and intellectual challenges involved include: expression of multimilligram quantities of recombinant protein for crystallization experiments, crystallization from detergent-solubilized protein solutions where the properties of the detergent may be as or more significant than those of the protein, and determination of a structure from crystals that may not be of very high quality. The 'payoff' of this research endeavor, however, is large; the structure of a membrane protein at atomic (or near-atomic) resolution is a significant achievement.

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Selected Publications

  • Pryor E, Wiener M. A critical evaluation of in silico methods for detection of membrane protein intrinsic disorder. Biophysical journal. 2014;106(8): 1638-49. PMID: 24739163 | PMCID: PMC4008797
  • Vergis J, Wiener M. The variable detergent sensitivity of proteases that are utilized for recombinant protein affinity tag removal. Protein expression and purification. 2011;78(2): 139-42. PMID: 21539919 | PMCID: PMC3130611
  • Wiener M, Horanyi P. How hydrophobic molecules traverse the outer membranes of gram-negative bacteria. Proceedings of the National Academy of Sciences of the United States of America. 2011;108(27): 10929-30. PMID: 21693645 | PMCID: PMC3131365
  • Freed D, Horanyi P, Wiener M, Cafiso D. Conformational exchange in a membrane transport protein is altered in protein crystals. Biophysical journal. 2010;99(5): 1604-10. PMID: 20816073 | PMCID: PMC2931748
  • Vergis J, Purdy M, Wiener M. A high-throughput differential filtration assay to screen and select detergents for membrane proteins. Analytical biochemistry. 2010;407(1): 1-11. PMID: 20667442
  • When worlds colloid. Protein science : a publication of the Protein Society. 2006;15(12): 2679-81. PMID: 17132858 | PMCID: PMC2242446
  • Chimento D, Kadner R, Wiener M. Comparative structural analysis of TonB-dependent outer membrane transporters: implications for the transport cycle. Proteins. 2005;59(2): 240-51. PMID: 15739205
  • Mohanty A, Wiener M. Membrane protein expression and production: effects of polyhistidine tag length and position. Protein expression and purification. 2004;33(2): 311-25. PMID: 14711520
  • Chimento D, Kadner R, Wiener M. The Escherichia coli outer membrane cobalamin transporter BtuB: structural analysis of calcium and substrate binding, and identification of orthologous transporters by sequence/structure conservation. Journal of molecular biology. 2003;332(5): 999-1014. PMID: 14499604
  • Chimento D, Mohanty A, Kadner R, Wiener M. Substrate-induced transmembrane signaling in the cobalamin transporter BtuB. Nature structural biology. 2003;10(5): 394-401. PMID: 12652322
  • Kurisu G, Zakharov S, Zhalnina M, Bano S, Eroukova V, Rokitskaya T, Antonenko Y, Wiener M, Cramer W. The structure of BtuB with bound colicin E3 R-domain implies a translocon. Nature structural biology. 2003;10(11): 948-54. PMID: 14528295
  • Mohanty A, Bishop C, Bishop T, Wimley W, Wiener M. Enzymatic E-colicins bind to their target receptor BtuB by presentation of a small binding epitope on a coiled-coil scaffold. The Journal of biological chemistry. 2003;278(42): 40953-8. PMID: 12902336