The Russell group leads development of a new variable-temperature ESI device for solution-phase studies of cold- and heat-induced folding, denaturation and self-assembly of proteins and protein complexes.

Recently the P41 Team has developed a new variable-temperature ESI device for solution-phase studies of cold- and heat-induced folding, denaturation and self-assembly of proteins and protein complexes. Using this device, the sample solution contained within the ESI emitter can be varied from 275K to 373K, which allows for direct sample of the effects of the solution environment (Gibbs free energy) on the structure/conformational preferences of the sample. The capabilities of the vT-ESI source have been demonstrated using model proteins (ubiquitin and human frataxin) and large protein complexes (GroEL, GroES complexes and the effects of ligands on the structure and stability of the intact GroEL/GroES complex. The vT-ESI source design and materials have been disseminated to a number of research groups and collaborators, including Arthur Laganowsky (Texas A&M University), Vicki Wysocki (The Ohio State University), David Clemmer (University of Indiana), Joseph S. Beckman (Oregon State University and eMSions), and Jennifer Brodbelt (University of Texas).