Decomposition of Charge-State Distributions for Better Understanding of Electrospray Mass Spectra of Bioorganic Compounds. Part 2: Application of the Method
Restricted accessResearch articleFirst published online June, 2009
Decomposition of Charge-State Distributions for Better Understanding of Electrospray Mass Spectra of Bioorganic Compounds. Part 2: Application of the Method
The results of the analysis of electrospray mass spectra of β-endorphin and chicken egg lysozyme in different conditions of data acquisition using the method described in Part 1 of the work are reported. At least partial unfolding during the process of ion formation in the electrospray ion source of an initially native biomolecule of lyzozyme in solution should supposedly explain the received set of probabilities of proton retention by basic and acidic residues of this molecule for all considered conditions of data acquisition.
LehningerA.L., Principles of Biochemistry.Worth Publishers, Inc., New York, USA (1982).
2.
DodonovA.KozlovskyV.LobodaA.RaznikovV.SulimenkovI.TolmachevA.KraftA.WollnikH., “A new technique for decomposition of selected ions in molecule ion reactor coupled with ortho-time-of-flight mass spectrometry”, Rapid Commun. Mass Spectrom.11, 1649 (1997). doi: 10.1002/(SICI)1097-0231(19971015)11:15<1649::AID-RCM67>3.0.CO;2-T
3.
BleiholderCh.SuhaiS.PaizsB., “Revising the proton affinity scale of the naturally occuring α-amino acids”, J. Am. Soc. Mass Spectrom.17, 1275 (2006). doi: 10.1016/j.jasms.2006.05.010
4.
MirgorodskayaO.A.ShevchenkoA.A.ChernushevichI.V.DodonovA.F.MiroshnikovA.I., “Electrospray ionization time-of-flight mass spectrometry in protein chemistry”, Anal. Chem.66, 99 (1994). doi: 10.1021/ac00073a018
5.
KellyM.A.VestlingM.M.FenselauC.C.SmithP.B., “Electrospray analysis of proteins: A comparison of positive-ion and negative-ion mass spectra at high and low pH”, Org. Mass Spectrom.27, 1143 (1992). doi: 10.1002/oms.1210271028
6.
PrakashH.MazumdarS., “Direct correlation of the crystal structure of proteins with the maximum positive and negative charge states of gaseous protein ions produced by electrospray ionization”, J. Am. Soc. Mass Spectrom.16, 1409 (2005). doi: 10.1016/j.jasms.2005.04.002
7.
OvchinnikovYu.A., Bioorganic Chemistry.Prosveshchenie, Moscow, Russia (1987), (in Russian).
8.
McAllisterC.KarymovM.KawanoY.LushnikovA.Y.MikheikinA.UverskyV.N.LyubchenkoY.L., “Protein interactions and misfolding analyzed by AFM force spectroscopy”, J. Mol. Biol.354, 1028 (2005). doi: 10.1016/j.jmb.2005.10.012
9.
AbzalimovR.R.FrimpongA.K.KaltashovI.A., “Gas-phase processes and measurements of macromolecular properties in solution: On the possibility of false positive and false negative signals of protein unfolding”, Int. J. Mass Spectrom.253, 207 (2006). doi: 10.1016/j.ijms.2006.03.002
10.
NesatyyV.J.SuterM.J.-F., “On the conformation-dependent neutralization theory and charging of individual proteins and their non-covalent complexes in the gas phase”, J. Mass Spectrom.39, 93 (2004). doi: 10.1002/jms.522
11.
FrimpongA.K.AbzalimovR.R.EylesS.J.KaltashovI.A., “Gas-phase interference-free analysis of protein ion charge-state distribution; detection of small-scale conformation transitions accompanying pepsin inactivation”, Anal. Chem.79, 4154 (2007). doi: 10.1021/ac0704098
12.
LyT.JulianR.R., “Using ESI-MS to probe protein structure by site-specific noncovalent attachment of 18-crown-6”, J. Am. Soc. Mass Spectrom.17, 1209 (2006). doi: 10.1016/j.jasms.2006.05.007
