A high-field NMR spectrometer, operating at a 1H resonance frequency of 600 MHz and fully equipped for biomolecular applications, is requested to meet the needs of a broad group of biophysical and biochemical investigators at the Homewood campus at Johns Hopkins University. The requested instrumentation will be sited in a newly completed NMR Center, constructed in accordance with the University's long term goal of providing state-of-the-art capabilities for fundamental investigations of biomolecular structure and dynamics. This instrumentation will significantly benefit the research programs of seven faculties from the Departments of Biology, Biophysics, and Chemistry, of which six are NIH-funded. A range of projects of biological, biophysical, and chemical significance are described: (1) Structure and dynamics studies of proteins involved in mitochondrial division. (2) NMR studies of macromolecular structure and dynamics and its relationship to biological function. (3) Long range effects of amino acid polymorphisms and mutations causing drug-resistant in the HIV-1 protease. (4) Structural and energetic principles of membrane proteins. (5) Correlation between structure and energy in proteins. (6) Structure determination of the DNA-binding domain of AraC and dynamics in the presence and absence of its cognate DNA. (7) Thermodynamic analysis of backbone and side chain dynamics of DNA binding proteins in the presence and absence of DNA.
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| Thuduppathy, Guruvasuthevan R; Terrones, Oihana; Craig, Jeffrey W et al. (2006) The N-terminal domain of Bcl-xL reversibly binds membranes in a pH-dependent manner. Biochemistry 45:14533-42 |
