User:Austin G. Meyer: Difference between revisions

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==Publications==
==Publications==
'''2014'''
'''2014'''
# A. Shahmoradi, D. K. Sydykova, S. J. Spielman, E. L. Jackson, E. T. Dawson, A. G. Meyer, and C. O. Wilke (submitted to Journal of Molecular Evolution). Predicting evolutionary site variability from structure in viral proteins: buriedness, flexibility, and design. [http://biorxiv.org/content/early/2014/04/24/004481 biorxiv.org/content/early/2014/04/24/004481]
# V. Sridhara, A. G. Meyer, J. E. Barrick, P. Ravikumar, D. Segre, and C. O. Wilke (submitted to PLOS ONE). Predicting bacterial growth conditions from metabolic output by flux balance analysis. [http://biorxiv.org/content/early/2014/01/31/002287 biorxiv.org/content/early/2014/01/31/002287]
# V. Sridhara, A. G. Meyer, J. E. Barrick, P. Ravikumar, D. Segre, and C. O. Wilke (submitted to PLOS ONE). Predicting bacterial growth conditions from metabolic output by flux balance analysis. [http://biorxiv.org/content/early/2014/01/31/002287 biorxiv.org/content/early/2014/01/31/002287]
# A. Shahmoradi, D. K. Sydykova, S. J. Spielman, E. L. Jackson, E. T. Dawson, A. G. Meyer, and C. O. Wilke (accepted to Journal of Molecular Evolution). Predicting evolutionary site variability from structure in viral proteins: buriedness, flexibility, and design. [http://biorxiv.org/content/early/2014/04/24/004481 biorxiv.org/content/early/2014/04/24/004481]
# A. G. Meyer, S. L. Sawyer, A. D. Ellington, and C. O. Wike (2014). Analyzing Machupo virus-receptor binding by molecular dynamics simulations. PeerJ, 2:e266. [http://dx.doi.org/10.7717/peerj.266 doi:10.7717/peerj.266]
# A. G. Meyer, S. L. Sawyer, A. D. Ellington, and C. O. Wike (2014). Analyzing Machupo virus-receptor binding by molecular dynamics simulations. PeerJ, 2:e266. [http://dx.doi.org/10.7717/peerj.266 doi:10.7717/peerj.266]
# K. Fuson, A. Rice, R. Mahling, A. Snow, K. Nayak, P. Shanbhogue, A. G. Meyer, G. Redpath, A. Hinderliter, S. T. Cooper and R. B. Sutton (2014). Alternate splicing of dysferlin C2A confers Ca2+-dependent and Ca2+-independent binding for membrane repair. Structure. [http://dx.doi.org/10.1016/j.str.2013.10.001 doi:10.1016/j.str.2013.10.001]
# K. Fuson, A. Rice, R. Mahling, A. Snow, K. Nayak, P. Shanbhogue, A. G. Meyer, G. Redpath, A. Hinderliter, S. T. Cooper and R. B. Sutton (2014). Alternate splicing of dysferlin C2A confers Ca2+-dependent and Ca2+-independent binding for membrane repair. Structure. [http://dx.doi.org/10.1016/j.str.2013.10.001 doi:10.1016/j.str.2013.10.001]

Revision as of 22:46, 30 August 2014

Contact Info

Austin G. Meyer (In Taos, NM)

Summary

I am currently in Austin, TX finishing up my PhD in Biochemistry. I will be returning to medical school full time in the summer of 2015 at Texas Tech University Health Sciences Center.

I am member of the lab of Dr. Claus Wilke at the University of Texas at Austin.

Visit my research website here.

My personal website is generally kept more up to date and in depth on my work.

Education

  • In Progress (2017), MD, Texas Tech University Health Sciences Center
  • In Progress (2014), PhD Biochemistry, University of Texas at Austin
  • 2010, MS Structural Biology, Texas Tech University Health Sciences Center
  • 2008, BS Physics, Texas Tech University
  • 2008, BA Philosophy, Texas Tech University

Research interests

  1. Quantitative Biology - In particular modeling biological phenomena and making predictions from simulations.
  2. Structural Biology and Biophysics
  3. Bio-medical Data Science - At the intersection of traditional fields like biology, medicine, statistics, and computer science. I think this will be the next revolution in science and technology. We are already seeing steps in this direction with important data troves coming from the Affordable Care Act's electronic health record mandates and the 1000 genomes project.
  4. Experimental Molecular Biology and Molecular Evolution - Exploiting natural processes to technological ends.

Publications

2014

  1. V. Sridhara, A. G. Meyer, J. E. Barrick, P. Ravikumar, D. Segre, and C. O. Wilke (submitted to PLOS ONE). Predicting bacterial growth conditions from metabolic output by flux balance analysis. biorxiv.org/content/early/2014/01/31/002287
  2. A. Shahmoradi, D. K. Sydykova, S. J. Spielman, E. L. Jackson, E. T. Dawson, A. G. Meyer, and C. O. Wilke (accepted to Journal of Molecular Evolution). Predicting evolutionary site variability from structure in viral proteins: buriedness, flexibility, and design. biorxiv.org/content/early/2014/04/24/004481
  3. A. G. Meyer, S. L. Sawyer, A. D. Ellington, and C. O. Wike (2014). Analyzing Machupo virus-receptor binding by molecular dynamics simulations. PeerJ, 2:e266. doi:10.7717/peerj.266
  4. K. Fuson, A. Rice, R. Mahling, A. Snow, K. Nayak, P. Shanbhogue, A. G. Meyer, G. Redpath, A. Hinderliter, S. T. Cooper and R. B. Sutton (2014). Alternate splicing of dysferlin C2A confers Ca2+-dependent and Ca2+-independent binding for membrane repair. Structure. doi:10.1016/j.str.2013.10.001

2013

  1. M. Tien, A. G. Meyer, D. K. Sydykova, S. J. Spielman, and C. O. Wilke (2013). Maximum allowed solvent accessibilities of residues in proteins. PLOS ONE. doi:10.1371/journal.pone.0080635
  2. M. Tien, D. K. Sydykova, A. G. Meyer, and C. O. Wilke (2013). A simple Python library to generate model peptides. PeerJ, 1:e80. doi:10.7717/peerj.80
  3. A. G. Meyer, E. T. Dawson, and C. O. Wilke (2013). Cross-species comparison of site-specific evolutionary-rate variation in influenza hemagglutinin. Philosophical Transactions of the Royal Society B. doi:10.1098/rstb.2012.033
  4. A. G. Meyer and C. O. Wilke (2013). Integrating sequence variation and protein structure to identify sites under selection. Molecular Biology and Evolution. doi:10.1093/molbev/mss217

2012

  1. M. P. Scherrer, A. G. Meyer and C. O. Wilke (2012). Modeling coding-sequence evolution within the context of residue solvent accessibility. BMC Evolutionary Biology. doi:10.1186/1471-2148-12-179
  2. A. Reba, A. G. Meyer and J. E. Barrick (2012) Computational tests of a thermal cycling strategy to isolate more complex functional nucleic acid motifs from random sequence pools by in vitro selection. In: C. Adami et al. (eds.). Artificial Life XIII: Proceedings of the Thirteenth International Conference on the Synthesis and Simulation of Living Systems. pp 473-480. Cambridge, MA: MIT Press. Awarded Best Synthetic Biology Paper. doi:10.7551/978-0-262-31050-5-ch062

Before 2012

  1. Y. G. Celebi, R. L. Lichti, H. N. Bani-Salameh, A. G. Meyer, B. R. Carroll, J. E. Vernon, P. J. C. King and S. F. J. Cox (2009). Muonium transitions in 4H silicon carbide. Physica B, 404, 845-84. doi:10.1016/j.physb.2008.11.155
  2. H. N. Bani-Salameh, A. G. Meyer, B. R. Carroll, R. L. Lichti, K. H. Chow, P. J. C. King and S. F. J. Cox (2007). Charge-state transitions of muonium in 6H silicon carbide. Physica B, 401-402, 631-634. doi:10.1016/j.physb.2007.09.039