Emergency BU Alert BU Medical Campus OPEN Jan. 28, 2015 Boston University Medical Campus will be open Wednesday, Jan. 28, 2015. BUSM classes will be held as scheduled. Staff should check with their managers regarding work schedules. Medical, PA and GMS students who are assigned to inpatient services or clinics are expected to be present, if possible. Students who are assigned to outpatient services should check with their course director or the policy at the clinical site. GMS classes are canceled. Staff should check with their manager regarding their work schedules. The Henry M. Goldman School of Dental Medicine will follow normal school hours. All Patient Treatment Centers will be open for patient care and all classes will be held as scheduled. BU School of Public Health classes are canceled; SPH non-essential staff may telecommute. Employees who are part of the BUMC parking program should park in your assigned lot or garage. The Boston parking ban is still in effect. For updated information, please call the weather/emergency hotline at 617-638-6886 or visit the BU Emergency Communications website at http://www.bu.edu/ehs/comm/

Circular Dichroism Spectrophotometer

An upgraded circular dichroism spectrometer, the AVIV 62 DS, is supported by the Department. Thermoelectric temperature control enables data collection in a broad range of temperatures and heating/cooling rates. Automated data collection in the far-UV (185-250 nm) and near-UV CD (250-360 nm) can be carried out as a function of wavelength, temperature or time, thus allowing protein secondary and tertiary structural analysis, thermodynamic analysis, and kinetic studies of protein folding/unfolding transitions. Data collection, processing and display are computer-controlled. Software packages LINEQ and ProtCD with a variety of structural data bases are available for the quantitative secondary structural analysis by CD spectral deconvolution.

In addition, we maintain a state-of-the-art AVIV 215 CD spectrometer with an automatic titrator for quantitative analysis of protein conformation, folding/unfolding transitions, and protein-ligand interactions. The fluorescence attachment on this instrument is used to record changes in the intrinsic protein fluorescence or to monitor heat-induced changes in the light scattering in aggregating proteins or lipid-protein complexes.

July 13, 2011
Primary teaching affiliate
of BU School of Medicine