History | Facilities | Alumni

The Thomas C. Jenkins Department of Biophysics is located on the Homewood Campus of Johns Hopkins University in Baltimore, Maryland. Jenkins Hall, which houses the Biophysics Department, is a modern, recently renovated research and teaching building. The Jenkins computer room has 15 G-5 iMacs and an LCD projector.  Jenkins Hall also has a Scyld Beowulf cluster with 34 slave nodes.  The Department owned Hewlett Packard Designjet 800PS “poster printer” continues to be a tremendous help to students and faculty in presenting their research at the University and at professional meetings.

It is a short walk to the Departments of Biology and Chemistry, with which we work very closely. There is a wide variety of state-of-the-art, shared facilities available, some of which are discussed below.

Although the research programs of the many faculty and students are diverse and varied, there are several recurring themes that underlie these different research programs. The existence of these common underlying themes and interests enhances interaction between research laboratories, and helps give the Department a leading status in these areas.

One such area is high-resolution structure determination of macromolecules. Most of the laboratories in the Department of Biophysics are either directly involved in determining the structure of proteins and nucleic acids, or are using high-resolution structures to illuminate their own work. The Department houses a new X-ray crystallography facility for macromolecular structure determination. This multi-user facility is shared by a number of laboratories, and provides ample access to all members of the Department. The adjacent Homewood Campus NMR facility became operational in October 2003. It will house five high field NMR spectrometers. Currently (Spring 2006), it has two Bruker Advance 600 MHz spectrometer and a Varian Inova 800 MHz spectrometer. Both will be equipped with cryogenic probes by the end of 2006.

Another common research theme is determination of the forces and energetics that determine macromolecular structure and function. Topics such as experimental studies of electrostatic and solvent interactions, and computational molecular and statistical mechanical analysis are prevalent in many laboratories in the Department. Students have access to two of the finest microcalorimetry laboratories in the field, state-of-the-art fluorescence and circular dichroism spectrophotometers. In addition, students can use EPR, NMR, and mass spectrometry facilities in the neighboring Department of Chemistry. Advanced computing facilities housed within the Department are available to students twenty-four hours a day.

A third common research theme is the study of macromolecular assembly, allostery, and regulation. Departmental laboratories are studying the kinetics and energetics of RNA folding, nucleoprotein complexes of viruses, ribosomes, and nucleosomes, DNA-protein interactions, hemoglobin allostery and polymerization, interactions between designer drugs and their targets, and complexes of signal transduction proteins. Research in this area is facilitated by a new, shared, analytical ultracentrifugation facility.

Finally, we are continuing a long departmental tradition of providing students with training in quantitative physiology, in which the principles of molecular biophysics are applied to complex biological environments. Areas of research include mechanisms of immunity and pathogenesis in mucosal environments, molecular and biophysical mechanisms of cell transformations, and associative learning.