The Houston Area Molecular Biophysics Program (HAMBP) has guided and led research training in molecular biophysics for PhD students in the Houston-Galveston area since 1989. A five-year renewal with one additional slot (10 total) is sought to allow continued excellence and innovation in training outstanding students interested in working at the cutting edges of this increasingly important field. Under the direction of the program director and a steering committee with representatives from each of five graduate schools of the Gulf Coast Consortia (Baylor College of Medicine, Rice University, University of Texas MD Anderson Cancer Center/University of Texas Health Science Center-Houston, University of Texas Medical Branch at Galveston, and University of Houston) the program provides didactic and seminar courses, two local annual research conferences with trainee talks and poster sessions, monthly trainee meetings, professional/career development seminars, attendance at national meetings, and annual presentation and review of trainee research progress. All students are required to participate in training in the responsible conduct of research and workshops in rigor and reproducibility. Mentors include 39 faculty members at six institutions, affiliated with 14 different departments and 4 interdepartmental graduate programs. These faculty have exemplary training and research records, as well as strong research funding. They have trained 191 predocs and 229 postdocs over the past 10 years, and continue to be active, with 106 predocs and 76 postdocs currently in their labs. Our predoctoral trainees will have completed one year of study and have selected a major thesis advisor at one of the participating institutions before joining HAMBP. Trainees are selected in a highly competitive process from students whose projects in mentors' laboratories provide training in molecular biophysics. While trainee selection is based on merit, the program is committed to enhancing diversity and has been very successful in recruiting and retaining members of underrepresented groups. Research strengths include x-ray crystallography, macromolecular NMR, cryo-electron microscopy, a wide range of spectroscopic and microscopic techniques, single molecule methods, computational biophysics, membrane biophysics, protein folding, nucleic acid structure and ultrastructure, thermodynamics, kinetics and mechanistic enzymology. Supported students who complete the program publish an average of 3 papers from their thesis research, including many in high impact journals, and go on to successful, research-focused careers in academia, industry, government agencies, and private organizations. The heavy involvement of institutions of the Texas Medical Center and the University of Texas Medical Branch at Galveston ensures that students are involved in and exposed to research relevant to human health. The quantitative and interdisciplinary skills that are emphasized in the program are critical for advancing biomedical research and making breakthroughs in our understanding of human disease processes and in the design of new therapeutics and diagnostics.

Public Health Relevance

The Houston Area Molecular Biophysics Program prepares Ph.D. students for research applying the principles of physics to important medical problems and to the basic biology underlying medical research. Training in Molecular Biophysics and the quantitative and interdisciplinary skills emphasized in the program enable research careers leading to fundamental understanding of human disease and development of innovative approaches to diagnostics, therapeutics, and disease prevention. Biophysics provides tools used by all specialties in biomedical research and in medical practice.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Institutional National Research Service Award (T32)
Project #
5T32GM008280-32
Application #
9957101
Study Section
NIGMS Initial Review Group (TWD)
Program Officer
Flicker, Paula F
Project Start
1988-09-30
Project End
2024-06-30
Budget Start
2020-07-01
Budget End
2021-06-30
Support Year
32
Fiscal Year
2020
Total Cost
Indirect Cost
Name
Baylor College of Medicine
Department
Biochemistry
Type
Schools of Medicine
DUNS #
051113330
City
Houston
State
TX
Country
United States
Zip Code
77030
Zegarra, Fabio C; Homouz, Dirar; Eliaz, Yossi et al. (2018) Impact of hydrodynamic interactions on protein folding rates depends on temperature. Phys Rev E 97:032402
Young, M; Dahoun, T; Sokrat, B et al. (2018) Computational design of orthogonal membrane receptor-effector switches for rewiring signaling pathways. Proc Natl Acad Sci U S A 115:7051-7056
Guo, Hou-Fu; Tsai, Chi-Lin; Terajima, Masahiko et al. (2018) Pro-metastatic collagen lysyl hydroxylase dimer assemblies stabilized by Fe2+-binding. Nat Commun 9:512
Chen, Jinjun; Li, Lingyong; Chen, Shao-Rui et al. (2018) The ?2?-1-NMDA Receptor Complex Is Critically Involved in Neuropathic Pain Development and Gabapentin Therapeutic Actions. Cell Rep 22:2307-2321
Nguyen, Dan; Iwahara, Junji (2018) Impact of two-bond 15N-15N scalar couplings on 15N transverse relaxation measurements for arginine side chains of proteins. J Biomol NMR 71:45-51
Cheung, Margaret S; Gasic, Andrei G (2018) Towards developing principles of protein folding and dynamics in the cell. Phys Biol 15:063001
Thomas, Emily E; Pandey, Naresh; Knudsen, Sarah et al. (2017) Programming Post-Translational Control over the Metabolic Labeling of Cellular Proteins with a Noncanonical Amino Acid. ACS Synth Biol 6:1572-1583
Nguyen, Dan; Hoffpauir, Zoe A; Iwahara, Junji (2017) Internal Motions of Basic Side Chains of the Antennapedia Homeodomain in the Free and DNA-Bound States. Biochemistry 56:5866-5869
Nguyen, Dan; Lokesh, Ganesh L R; Volk, David E et al. (2017) A Unique and Simple Approach to Improve Sensitivity in 15N-NMR Relaxation Measurements for NH?? Groups: Application to a Protein-DNA Complex. Molecules 22:
Brown, Aaron J; Sepuru, Krishna Mohan; Rajarathnam, Krishna (2017) Structural Basis of Native CXCL7 Monomer Binding to CXCR2 Receptor N-Domain and Glycosaminoglycan Heparin. Int J Mol Sci 18:

Showing the most recent 10 out of 123 publications