Electron capture dissociation of gaseous multiply charged ions by Fourier-transform ion cyclotron resonance.
Fourier-transform ion cyclotron resonance instrumentation is uniquely applicable to an unusual new ion chemistry, electron capture dissociation (ECD). This causes nonergodic dissociation of far larger molecules (42 kDa) than previously observed (<1 kDa), with the resulting unimolecular ion chemistry also unique because it involves radical site reactions for similarly larger ions. ECD is highly complementary to the well known energetic methods for multiply charged ion dissociation, providing much more extensive protein sequence information, including the direct identification of N- versus C-terminal fragment ions. Because ECD only excites the molecule near the cleavage site, accompanying rearrangements are minimized. Counterintuitively, cleavage of backbone covalent bonds of protein ions is favored over that of noncovalent bonds; larger (>10 kDa) ions give far more extensive ECD if they are first thermally activated. This high specificity for covalent bond cleavage also makes ECD promising for studying the secondary and tertiary structure of gaseous protein ions caused by noncovalent bonding.
McLafferty
F W
FW
Baker Chemistry Laboratory, Cornell University, Ithaca, New York 13853-1301, USA. fredwmel@aol.com
Horn
D M
DM
Breuker
K
K
Ge
Y
Y
Lewis
M A
MA
Cerda
B
B
Zubarev
R A
RA
Carpenter
B K
BK
D017357:Cyclotrons; D005583:Fourier Analysis; D013058:Mass Spectrometry / Q000295:instrumentation / Q000379:methods*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry; D020543:Proteome / Q000032:analysis; D020539:Sequence Analysis, Protein
D011506:Proteins; D020543:Proteome