Conformations and folding of lysozyme ions in vacuo.
Proton transfer reactivity of isolated charge states of the protein hen egg-white lysozyme shows that multiple distinct conformations of this protein are stable in the gas phase. The reactivities of the 9+ and 10+ charge state ions, formed by electrospray ionization of "native" (disulfide-intact) and "denatured" (disulfide-reduced) solutions, are consistent with values calculated for ions in their crystal structure and fully denatured conformations, respectively. Charge states below 8+ of both forms, formed by proton stripping, have similar or indistinguishable reactivities, indicating that the disulfide-reduced ions fold in the gas phase to a more compact conformation.
Gross
D S
DS
Department of Chemistry, University of California, Berkeley 94720, USA.
Schnier
P D
PD
Rodriguez-Cruz
S E
SE
Fagerquist
C K
CK
Williams
E R
ER
D000818:Animals; D002645:Chickens; D003461:Crystallography; D004220:Disulfides; D005260:Female; D005583:Fourier Analysis; D013058:Mass Spectrometry / Q000295:instrumentation / Q000379:methods; D009113:Muramidase / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D011522:Protons
D004220:Disulfides; D011522:Protons; D009113:Muramidase