Transfer of structural elements from compact to extended states in unsolvated ubiquitin.
Multidimensional ion mobility spectrometry techniques (IMS-IMS and IMS-IMS-IMS) combined with mass spectrometry are used to study structural transitions of ubiquitin ions in the gas phase. It is possible to select and activate narrow distributions of compact and partially folded conformation types and examine new distributions of structures that are formed. Different compact conformations unfold, producing a range of new partially folded states and three resolvable peaks associated with elongated conformers. Under gentle activation conditions, the final populations of the three elongated forms depend on the initial structures of the selected ions. This requires that some memory of the compact state (most likely secondary structure) is preserved along the unfolding pathway. Activation of selected, partially folded intermediates (formed from specific compact states) leads to elongated state populations that are consistent with the initial selected compact form-evidence that intermediates not only retain elements of initial structure but also are capable of transmitting structure to final states.
Koeniger
Stormy L
SL
Department of Chemistry, Indiana University, Bloomington, Indiana 47405, USA.
Merenbloom
Samuel I
SI
Sevugarajan
Sundarapandian
S
Clemmer
David E
DE
D007477:Ions / Q000737:chemistry; D044367:Phase Transition; D011487:Protein Conformation; D017510:Protein Folding; D012995:Solubility; D021241:Spectrometry, Mass, Electrospray Ionization; D053719:Tandem Mass Spectrometry / Q000379:methods; D025801:Ubiquitin / Q000737:chemistry*
D007477:Ions; D025801:Ubiquitin