Continued support is requested for an ongoing program of graduate research training in molecular biology and biophysics at the University of Oregon. This training activity is centered in the Institute of Molecular Biology, and also involves additional groups with related scientific interests. Funds are requested for 12 predoctoral positions, within a program that includes approximately 50 graduate students, 46 postdoctoral trainees, and 19 training faculty. The program places special emphasis on the control of gene expression and nucleic acid structure/function, molecular basis of signaling and cell function, protein structure and dynamics, and molecular approaches to development and differentiation. The basic aspect of the training is laboratory research carried out under the direction of a faculty member in the molecular biology and biophysics training program. Through this experience, the trainee becomes skilled at posing questions about fundamental biological processes and designing experiments to answer those questions. The training is augmented by formal courses offered by the Biology, Chemistry, and Physics Departments, by seminar programs that highlight current research in molecular biology, biophysics, and related disciplines, by the close involvement of a Thesis Advisory Committee, and by research seminar and journal club presentations by trainees. The training facilities include the laboratories of the faculty and support services such as the structural biology facility, the state of the art genomics and proteomics facilities, biophysical chemistry equipment facility, the media preparation facility, an electron, confocal and 2-photon microscope facility, and a polyclonal/monoclonal antibody facility. Major equipment is shared and housed in common space. The laboratories of most of the faculty are contiguous and in interconnected buildings. This arrangement fosters interactions and collaborations among faculty and students.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Institutional National Research Service Award (T32)
Project #
5T32GM007759-33
Application #
8101037
Study Section
National Institute of General Medical Sciences Initial Review Group (BRT)
Program Officer
Flicker, Paula F
Project Start
1979-07-01
Project End
2012-06-30
Budget Start
2011-07-01
Budget End
2012-06-30
Support Year
33
Fiscal Year
2011
Total Cost
$290,357
Indirect Cost
Name
University of Oregon
Department
Biochemistry
Type
Organized Research Units
DUNS #
948117312
City
Eugene
State
OR
Country
United States
Zip Code
97403
Phelps, Carey; Israels, Brett; Jose, Davis et al. (2017) Using microsecond single-molecule FRET to determine the assembly pathways of T4 ssDNA binding protein onto model DNA replication forks. Proc Natl Acad Sci U S A 114:E3612-E3621
Miranda, Rafael G; Rojas, Margarita; Montgomery, Michael P et al. (2017) RNA-binding specificity landscape of the pentatricopeptide repeat protein PPR10. RNA 23:586-599
Sackman, Andrew M; McGee, Lindsey W; Morrison, Anneliese J et al. (2017) Mutation-Driven Parallel Evolution during Viral Adaptation. Mol Biol Evol 34:3243-3253
Ewing, Simon A; Donor, Micah T; Wilson, Jesse W et al. (2017) Collidoscope: An Improved Tool for Computing Collisional Cross-Sections with the Trajectory Method. J Am Soc Mass Spectrom 28:587-596
Wheeler, Lucas C; Harms, Michael J (2017) Human S100A5 binds Ca2+ and Cu2+ independently. BMC Biophys 10:8
Plakos, Kory; DeRose, Victoria J (2017) Mapping platinum adducts on yeast ribosomal RNA using high-throughput sequencing. Chem Commun (Camb) 53:12746-12749
Wheeler, Lucas C; Donor, Micah T; Prell, James S et al. (2016) Multiple Evolutionary Origins of Ubiquitous Cu2+ and Zn2+ Binding in the S100 Protein Family. PLoS One 11:e0164740
Wheeler, Lucas C; Lim, Shion A; Marqusee, Susan et al. (2016) The thermostability and specificity of ancient proteins. Curr Opin Struct Biol 38:37-43
Lee, Wonbae; Gillies, John P; Jose, Davis et al. (2016) Single-molecule FRET studies of the cooperative and non-cooperative binding kinetics of the bacteriophage T4 single-stranded DNA binding protein (gp32) to ssDNA lattices at replication fork junctions. Nucleic Acids Res 44:10691-10710
McGee, Lindsey W; Sackman, Andrew M; Morrison, Anneliese J et al. (2016) Synergistic Pleiotropy Overrides the Costs of Complexity in Viral Adaptation. Genetics 202:285-95

Showing the most recent 10 out of 115 publications