This proposal requests funding for renewal of an NIH Training Program in Molecular Biophysics (the MBTP) at the University of Wisconsin-Madison. Molecular biophysics takes a quantitative, physical, non- phenomenological approach to biology that is firmly rooted in the principles of condensed-phase physics and physical chemistry. Biophysicists are driven primarily by their curiosity about how biological systems work at the molecular level. They are often responsible for development of state-of-the-art measurements that eventually enhance the capabilities of all biological scientists, including medical researchers. The MBTP trainees are a highly sought cohort of graduate students combining strength in mathematics and physical science with a genuine interest in complex biological systems. Our current trainees have a mean GRE Quantitative score of 778 on a scale of 80. The key elements in the Training Program are core coursework that ensures that all trainees have a firm grounding in physical and biological principles;strong, interdisciplinary research at the forefront of molecular biophysics;coursework and informal training in proper conduct of scientific research;and close interaction with a thesis/mentoring committee that is formed in the second year and maintains a strong connection with the trainee throughout the Ph.D. program. The UW- Madison offers a tremendous range of seminars, poster sessions, and auxiliary coursework that greatly enhance the scientific breadth of our trainees. The MBTP and Biophysics Graduate Degree Program (BGDP) have now operated for seven years under a unified administrative structure. A single Biophysics Steering Committee administers both the MBTP and the BGDP. We are working hard to create a coherent community of biophysics students on the UW-Madison campus. Requirements put in place ensure uniformity of the training experiences of all biophysics students on campus, both MBTP trainees (regardless of home department) and BGDP students. Through a common, weekly Biophysics Seminar class, poster sessions, Biophysics Evenings, all biophysics students share many opportunities to interact with faculty trainers and with each other. By leveraging existing connections with outreach programs already existing on campus and continuing with new stronger initiatives within the program, the MBTP trainers will enhance ongoing efforts to increase participation of underrepresented minority students in both the MBTP and the BGDP. To enforce accountability, any trainer who accepts a new trainee will be required to participate in one meaningful outreach activity each year. In the coming grant period, we also plan to improve self-evaluation of the effectiveness of the MBTP via exit interviews and a periodic survey of former trainees at least five years after their Ph.D.
There have been tremendous advances in the treatment of human disease and health related quality of life issues. At the same time, many challenges remain and the promise held by today's understanding requires well-trained researchers that will drive tomorrow's advances. The goal of the MBTP at the University of Wisconsin-Madison is to provide a training environment that produces young scientists to meet the challenges.
|Lee, Jung Ho; Okuno, Yusuke; Cavagnero, Silvia (2014) Sensitivity enhancement in solution NMR: emerging ideas and new frontiers. J Magn Reson 241:18-31|
|Laaser, Jennifer E; Skoff, David R; Ho, Jia-Jung et al. (2014) Two-dimensional sum-frequency generation reveals structure and dynamics of a surface-bound peptide. J Am Chem Soc 136:956-62|
|Trang, Vivian H; Rodgers, Margaret L; Boyle, Kevin J et al. (2014) Chemoenzymatic synthesis of bifunctional polyubiquitin substrates for monitoring ubiquitin chain remodeling. Chembiochem 15:1563-8|
|Larson, Joshua D; Rodgers, Margaret L; Hoskins, Aaron A (2014) Visualizing cellular machines with colocalization single molecule microscopy. Chem Soc Rev 43:1189-200|
|Sundlass, Nadia K; Eller, Chelcie H; Cui, Qiang et al. (2013) Contribution of electrostatics to the binding of pancreatic-type ribonucleases to membranes. Biochemistry 52:6304-12|
|Woys, Ann Marie; Mukherjee, Sudipta S; Skoff, David R et al. (2013) A strongly absorbing class of non-natural labels for probing protein electrostatics and solvation with FTIR and 2D IR spectroscopies. J Phys Chem B 117:5009-18|
|Shin, Young-Hee; Mortenson, David E; Satyshur, Kenneth A et al. (2013) Differential impact of * and ýý residue preorganization on */*/ýý-peptide helix stability in water. J Am Chem Soc 135:8149-52|
|Hayouka, Zvi; Mortenson, David E; Kreitler, Dale F et al. (2013) Evidence for phenylalanine zipper-mediated dimerization in the X-ray crystal structure of a magainin 2 analogue. J Am Chem Soc 135:15738-41|
|Johnson, Lisa M; Gellman, Samuel H (2013) ?-Helix mimicry with ?/?-peptides. Methods Enzymol 523:407-29|
|Johnson, Lisa M; Mortenson, David E; Yun, Hyun Gi et al. (2012) Enhancement of ýý-helix mimicry by an ýý/ýý-peptide foldamer via incorporation of a dense ionic side-chain array. J Am Chem Soc 134:7317-20|
Showing the most recent 10 out of 65 publications