Several pieces of equipment in this facility provide an integrated set of different biophysical approaches for studies of macromolecular structure and interactions. The below instrumentation is available as of April 2016.
For further information, please contact Diane Beckford at firstname.lastname@example.org or at 212.413.3221.
This instrument uses changes in thermophoretic mobility – the migration of macromolecules into or away from a zone with elevated temperature – to characterize binding reactions. Advantages of this instrument include low sample consumption (ca. 100 microliters of low micromolar protein samples) and speed of measurement (under one hour for 16 point titration curve).
Provides independent measurements of molar mass and size of macromolecules in solution, particularly when coupled with Superdex 75 or Superdex 200 gel filtration chromatography (SEC-MALS).
Utilized for studies of protein secondary and tertiary structure, this spectrometer can detect changes in either circular dichroism (monitoring protein backbone environments) or fluorescence (monitoring Trp sidechains and other fluorescent groups). Accessories allow variable temperature operation, automated titrations and stopped-flow experiments.