Resolution and structural transitions of elongated states of ubiquitin

被引:95
作者
Koeniger, Stormy L. [1 ]
Clemmer, David E. [1 ]
机构
[1] Indiana Univ, Dept Chem, Bloomington, IN 47405 USA
关键词
D O I
10.1016/j.jasms.2006.09.025
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Electrospray ionization, combined with two-dimensional ion mobility spectrometry and mass spectrometry, is used to produce, select, and activate distributions of elongated ions, [M + 11H](11+) to [M + 13H](13+), of ubiquitin. The analysis makes it possible to examine state-to-state transitions for structural types, and transition diagrams associated with the efficiencies of structural changes are presented. The +11 and +12 charge states can form four resolvable states while only one state is formed for [M + 13H](13+). Some conformations, which appear to belong to the same family based on mobility analysis of different charge states, undergo similar transitions, others do not. Activation of ions that exist in low-abundance conformations, having mobilities that fall in between sharp peaks associated with higher abundances species, shows that the low-abundance forms undergo efficient (similar to 90 to 100%) conversion into states associated with well-defined peaks. This efficiency is significantly higher than the similar to 10 to 60% efficiency of transitions of structures associated with well-defined peaks. The formation of sharp features from a range of low-intensity species with different cross sections indicates that large regions of conformation space must be unfavorable or inaccessible in the gas phase. These results are compared with several previous IMS measurements of this system as well as information about gas-phase structure provided by other techniques.
引用
收藏
页码:322 / 331
页数:10
相关论文
共 77 条
[1]   Evidence for unfolding and refolding of gas-phase cytochrome c ions in a Paul trap [J].
Badman, ER ;
Myung, S ;
Clemmer, DE .
JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY, 2005, 16 (09) :1493-1497
[2]   Dissociation of different conformations of ubiquitin ions [J].
Badman, ER ;
Hoaglund-Hyzer, CS ;
Clemmer, DE .
JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY, 2002, 13 (06) :719-723
[3]   Monitoring structural changes of proteins in an ion trap over ∼10-200 ms:: Unfolding transitions in cytochrome c ions [J].
Badman, ER ;
Hoaglund-Hyzer, CS ;
Clemmer, DE .
ANALYTICAL CHEMISTRY, 2001, 73 (24) :6000-6007
[4]   Is it biologically relevant to measure the structures of small peptides in the gas-phase? [J].
Barran, PE ;
Polfer, NC ;
Campopiano, DJ ;
Clarke, DJ ;
Langridge-Smith, PRR ;
Langley, RJ ;
Govan, JRW ;
Maxwell, A ;
Dorin, JR ;
Millar, RP ;
Bowers, MT .
INTERNATIONAL JOURNAL OF MASS SPECTROMETRY, 2005, 240 (03) :273-284
[5]   Amyloid β-protein monomer structure:: A computational and experimental study [J].
Baumketner, A ;
Bernstein, SL ;
Wyttenbach, T ;
Bitan, G ;
Teplow, DB ;
Bowers, MT ;
Shea, JE .
PROTEIN SCIENCE, 2006, 15 (03) :420-428
[6]   Amyloid β-protein:: Monomer structure and early aggregation states of Aβ42 and its Pro19 alloform [J].
Bernstein, SL ;
Wyttenbach, T ;
Baumketner, A ;
Shea, JE ;
Bitan, G ;
Teplow, DB ;
Bowers, MT .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2005, 127 (07) :2075-2084
[7]   The thermal unfolding of native cytochrome c in the transition from solution to gas phase probed by native electron capture dissociation [J].
Breuker, K ;
McLafferty, FW .
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2005, 44 (31) :4911-4914
[8]  
Cassady CJ, 1996, J MASS SPECTROM, V31, P247, DOI 10.1002/(SICI)1096-9888(199603)31:3<247::AID-JMS285>3.0.CO
[9]  
2-L
[10]   DEPROTONATION REACTIONS OF MULTIPLY PROTONATED UBIQUITIN IONS [J].
CASSADY, CJ ;
WRONKA, J ;
KRUPPA, GH ;
LAUKIEN, FH .
RAPID COMMUNICATIONS IN MASS SPECTROMETRY, 1994, 8 (05) :394-400