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Ion mobility mass spectrometry of proteins and proteinassemblies

Uetrecht, Charlotte, Rose, Rebecca J., van Duijn, Esther, Lorenzen, Kristina, Heck, Albert J. R.·2010·Chem. Soc. Rev.

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Abstract

Traditionally, mass spectrometry has been a powerful analytical method enabling the structural analysis of small molecules, and later on peptides and proteins. With the advent of native mass spectrometry, using a combination of electrospray ionisation and time of flight analysis, mass spectrometry could also be applied to the mass determination of large protein complexes such as ribosomes and whole viruses. More recently, ion mobility has been coupled to mass spectrometry providing a new dimension in the analysis of biomolecules, with ion mobility separating ions according to differences in size and shape. In the context of native mass spectrometry, ion mobility mass spectrometry opens up avenues for the detailed structural analysis of large and heterogeneous protein complexes, providing information on the stoichiometry, topology and cross section of these assemblies and their composite subunits. With these characteristics, ion mobility mass spectrometry offers a complementary tool in the context of structural biology. Here, we critically review the development, instrumentation, approaches and applications of ion mobility in combination with mass spectrometry, focusing on the analysis of larger proteins and protein assemblies (185 references).

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Time-of-Flight Mass Spectrometer with Improved Resolution
Wiley, W. C., & McLaren, I. H. (1955) · Review of Scientific Instruments · doi:10.1063/1.1715212 · Cited by 3,678
Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
Rosenthal, P. B., & Henderson, R. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.07.013 · Cited by 2,416
Structural Basis of Transcription: RNA Polymerase II at 2.8 Ångstrom Resolution
Cramer, P., Bushnell, D. A., & Kornberg, R. D. (2001) · Science · doi:10.1126/science.1059493 · Cited by 1,247
Studying noncovalent protein complexes by electrospray ionization mass spectrometry
Loo, J. A. (1997) · Mass Spectrometry Reviews · doi:10.1002/(sici)1098-2787(1997)16:1<1::aid-mas1>3.0.co;2-l · Cited by 1,182
Ion mobility–mass spectrometry
Kanu, A. B., Dwivedi, P., Tam, M., Matz, L., & Hill, H. H. (2008) · Journal of Mass Spectrometry · doi:10.1002/jms.1383 · Cited by 1,154
Ion mobility–mass spectrometry analysis of large protein complexes
Ruotolo, B. T., Benesch, J. L. P., Sandercock, A. M., Hyung, S.-J., & Robinson, C. V. (2008) · Nature Protocols · doi:10.1038/nprot.2008.78 · Cited by 1,092
Structural Information from Ion Mobility Measurements: Effects of the Long-Range Potential
Mesleh, M. F., Hunter, J. M., Shvartsburg, A. A., Schatz, G. C., & Jarrold, M. F. (1996) · The Journal of Physical Chemistry · doi:10.1021/jp961623v · Cited by 1,043
An exact hard-spheres scattering model for the mobilities of polyatomic ions
Shvartsburg, A. A., & Jarrold, M. F. (1996) · Chemical Physics Letters · doi:10.1016/0009-2614(96)00941-4 · Cited by 819
An investigation of the mobility separation of some peptide and protein ions using a new hybrid quadrupole/travelling wave IMS/oa-ToF instrument
Pringle, S. D., Giles, K., Wildgoose, J. L., Williams, J. P., Slade, S. E., Thalassinos, K., Bateman, R. H., Bowers, M. T., & Scrivens, J. H. (2007) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2006.07.021 · Cited by 808
Native mass spectrometry: a bridge between interactomics and structural biology
Heck, A. J. R. (2008) · Nature Methods · doi:10.1038/nmeth.1265 · Cited by 766
Self-citation
Ion Mobility Measurements and their Applications to Clusters and Biomolecules
Clemmer, D. E., & Jarrold, M. F. (1997) · Journal of Mass Spectrometry · doi:10.1002/(sici)1096-9888(199706)32:6<577::aid-jms530>3.0.co;2-4 · Cited by 741
Applications of a travelling wave‐based radio‐frequency‐only stacked ring ion guide
Giles, K., Pringle, S. D., Worthington, K. R., Little, D., Wildgoose, J. L., & Bateman, R. H. (2004) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.1641 · Cited by 727
Analysis of protein complexes using mass spectrometry
Gingras, A.-C., Gstaiger, M., Raught, B., & Aebersold, R. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2208 · Cited by 708
Architecture of RNA Polymerase II and Implications for the Transcription Mechanism
Cramer, P., Bushnell, D. A., Fu, J., Gnatt, A. L., Maier-Davis, B., Thompson, N. E., Burgess, R. R., Edwards, A. M., David, P. R., & Kornberg, R. D. (2000) · Science · doi:10.1126/science.288.5466.640 · Cited by 627
Evidence for Macromolecular Protein Rings in the Absence of Bulk Water
Ruotolo, B. T., Giles, K., Campuzano, I., Sandercock, A. M., Bateman, R. H., & Robinson, C. V. (2005) · Science · doi:10.1126/science.1120177 · Cited by 596
Carbon cluster cations with up to 84 atoms: structures, formation mechanism, and reactivity
von Helden, G., Hsu, M. T., Gotts, N., & Bowers, M. T. (1993) · The Journal of Physical Chemistry · doi:10.1021/j100133a011 · Cited by 593
Predicting protein function from sequence and structure
Lee, D., Redfern, O., & Orengo, C. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2281 · Cited by 583
Investigation of intact protein complexes by mass spectrometry
Heck, A. J. R., & van den Heuvel, R. H. H. (2004) · Mass Spectrometry Reviews · doi:10.1002/mas.10081 · Cited by 583
Self-citation
Fundamentals of Traveling Wave Ion Mobility Spectrometry
Shvartsburg, A. A., & Smith, R. D. (2008) · Analytical Chemistry · doi:10.1021/ac8016295 · Cited by 534
Progress and challenges in protein structure prediction
Zhang, Y. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.02.004 · Cited by 506
Flexible ligand docking to multiple receptor conformations: a practical alternative
Totrov, M., & Abagyan, R. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.01.004 · Cited by 497
Naked Protein Conformations: Cytochrome c in the Gas Phase
Clemmer, D. E., Hudgins, R. R., & Jarrold, M. F. (1995) · Journal of the American Chemical Society · doi:10.1021/ja00145a037 · Cited by 491
Transition networks for modeling the kinetics of conformational change in macromolecules
Noé, F., & Fischer, S. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.01.008 · Cited by 481
HbVar: A relational database of human hemoglobin variants and thalassemia mutations at the globin gene server
Hardison, R. C., Chui, D. H. K., Giardine, B., Riemer, C., Patrinos, G. P., Anagnou, N., Miller, W., & Wajcman, H. (2002) · Human Mutation · doi:10.1002/humu.10044 · Cited by 439
Experimental evidence for the formation of fullerenes by collisional heating of carbon rings in the gas phase
von Helden, G., Gotts, N. G., & Bowers, M. T. (1993) · Nature · doi:10.1038/363060a0 · Cited by 423
Protein Structure in Vacuo: Gas-Phase Conformations of BPTI and Cytochrome c
Shelimov, K. B., Clemmer, D. E., Hudgins, R. R., & Jarrold, M. F. (1997) · Journal of the American Chemical Society · doi:10.1021/ja9619059 · Cited by 414
Protein Complexes in the Gas Phase: Technology for Structural Genomics and Proteomics
Benesch, J. L. P., Ruotolo, B. T., Simmons, D. A., & Robinson, C. V. (2007) · Chemical Reviews · doi:10.1021/cr068289b · Cited by 408
Peptides and Proteins in the Vapor Phase
Jarrold, M. F. (2000) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.51.1.179 · Cited by 361
The Role of Mass Spectrometry in Structure Elucidation of Dynamic Protein Complexes
Sharon, M., & Robinson, C. V. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.061005.090816 · Cited by 357
Three-Dimensional Ion Mobility/TOFMS Analysis of Electrosprayed Biomolecules
Hoaglund, C. S., Valentine, S. J., Sporleder, C. R., Reilly, J. P., & Clemmer, D. E. (1998) · Analytical Chemistry · doi:10.1021/ac980059c · Cited by 345
Amyloid β-Protein: Monomer Structure and Early Aggregation States of Aβ42 and Its Pro19Alloform
Bernstein, S. L., Wyttenbach, T., Baumketner, A., Shea, J.-E., Bitan, G., Teplow, D. B., & Bowers, M. T. (2005) · Journal of the American Chemical Society · doi:10.1021/ja044531p · Cited by 341
Deciphering Drift Time Measurements from Travelling Wave Ion Mobility Spectrometry-Mass Spectrometry Studies
Smith, D. P., Knapman, T. W., Campuzano, I., Malham, R. W., Berryman, J. T., Radford, S. E., & Ashcroft, A. E. (2009) · European Journal of Mass Spectrometry · doi:10.1255/ejms.947 · Cited by 334
Effect of the long-range potential on ion mobility measurements
Wyttenbach, T., von Helden, G., Batka, J. J., Carlat, D., & Bowers, M. T. (1997) · Journal of the American Society for Mass Spectrometry · doi:10.1016/s1044-0305(96)00236-x · Cited by 332
Anhydrous Protein Ions
Hoaglund-Hyzer, C. S., Counterman, A. E., & Clemmer, D. E. (1999) · Chemical Reviews · doi:10.1021/cr980139g · Cited by 320
Ion mobility–mass spectrometry: a new paradigm for proteomics
McLean, J. A., Ruotolo, B. T., Gillig, K. J., & Russell, D. H. (2005) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2004.10.003 · Cited by 309
Native protein mass spectrometry: from intact oligomers to functional machineries
Heuvel, R. H. V. D., & Heck, A. J. (2004) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2004.08.006 · Cited by 303
Self-citation
Ion Mobility Spectrometry in Analytical Chemistry
St. Louis, R. H., Hill, H. H., & Eiceman, G. A. (1990) · Critical Reviews in Analytical Chemistry · doi:10.1080/10408349008050848 · Cited by 302
High-resolution ion mobility measurements
Dugourd, P., Hudgins, R. R., Clemmer, D. E., & Jarrold, M. F. (1997) · Review of Scientific Instruments · doi:10.1063/1.1147873 · Cited by 299
Comparative modeling for protein structure prediction
Ginalski, K. (2006) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2006.02.003 · Cited by 296
Dimorphism of Hepatitis B Virus Capsids Is Strongly Influenced by the C-Terminus of the Capsid Protein
Zlotnick, A., Cheng, N., Conway, J. F., Booy, F. P., Steven, A. C., Stahl, S. J., & Wingfield, P. T. (1996) · Biochemistry · doi:10.1021/bi9604800 · Cited by 287
Origin of Asymmetric Charge Partitioning in the Dissociation of Gas-Phase Protein Homodimers
Jurchen, J. C., & Williams, E. R. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0211508 · Cited by 284
Preparing Protein Microarrays by Soft-Landing of Mass-Selected Ions
Ouyang, Z., Takáts, Z., Blake, T. A., Gologan, B., Guymon, A. J., Wiseman, J. M., Oliver, J. C., Davisson, V. J., & Cooks, R. G. (2003) · Science · doi:10.1126/science.1088776 · Cited by 277
Design of a new electrospray ion mobility mass spectrometer
Wyttenbach, T., Kemper, P. R., & Bowers, M. T. (2001) · International Journal of Mass Spectrometry · doi:10.1016/s1387-3806(01)00517-6 · Cited by 277
Electrospray Ionization High-Field Asymmetric Waveform Ion Mobility Spectrometry−Mass Spectrometry
Purves, R. W., & Guevremont, R. (1999) · Analytical Chemistry · doi:10.1021/ac981380y · Cited by 265
Mass spectrometric characterization of a high-field asymmetric waveform ion mobility spectrometer
Purves, R. W., Guevremont, R., Day, S., Pipich, C. W., & Matyjaszczyk, M. S. (1998) · Review of Scientific Instruments · doi:10.1063/1.1149255 · Cited by 265
Electrosonic Spray Ionization. A Gentle Technique for Generating Folded Proteins and Protein Complexes in the Gas Phase and for Studying Ion−Molecule Reactions at Atmospheric Pressure
Takáts, Z., Wiseman, J. M., Gologan, B., & Cooks, R. G. (2004) · Analytical Chemistry · doi:10.1021/ac049848m · Cited by 261
Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA
Antson, A. A., Dodson, E. J., Dodson, G., Greaves, R. B., Chen, X., & Gollnick, P. D. (1999) · Nature · doi:10.1038/45730 · Cited by 257
Collision cross sections for protein ions
Covey, T., & Douglas, D. J. (1993) · Journal of the American Society for Mass Spectrometry · doi:10.1016/1044-0305(93)85025-s · Cited by 253
Amyloid β‐protein monomer structure: A computational and experimental study
Baumketner, A., Bernstein, S. L., Wyttenbach, T., Bitan, G., Teplow, D. B., Bowers, M. T., & Shea, J. (2006) · Protein Science · doi:10.1110/ps.051762406 · Cited by 247
Ion mobility spectrometry: a review. Part 1. Structural analysis by mobility measurement
Creaser, C. S., Griffiths, J. R., Bramwell, C. J., Noreen, S., Hill, C. A., & Thomas, C. L. P. (2004) · The Analyst · doi:10.1039/b404531a · Cited by 235
Conformer-dependent proton-transfer reactions of ubiquitin ions
Valentine, S. J., Counterman, A. E., & Clemmer, D. E. (1997) · Journal of the American Society for Mass Spectrometry · doi:10.1016/s1044-0305(97)00085-8 · Cited by 230
Ion Mobility–Mass Spectrometry Reveals Long‐Lived, Unfolded Intermediates in the Dissociation of Protein Complexes
Ruotolo, B. T., Hyung, S., Robinson, P. M., Giles, K., Bateman, R. H., & Robinson, C. V. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200702161 · Cited by 229
LXXIV. A positive ray spectrograph
Aston, F. W. (1919) · The London Edinburgh and Dublin Philosophical Magazine and Journal of Science · doi:10.1080/14786441208636004 · Cited by 224
Tandem Mass Spectrometry Reveals the Quaternary Organization of Macromolecular Assemblies
Benesch, J. L. P., Aquilina, J. A., Ruotolo, B. T., Sobott, F., & Robinson, C. V. (2006) · Chemistry & Biology · doi:10.1016/j.chembiol.2006.04.006 · Cited by 222
A database of 660 peptide ion cross sections: Use of intrinsic size parameters for bona fide predictions of cross sections
Valentine, S. J., Counterman, A. E., & Clemmer, D. E. (1999) · Journal of the American Society for Mass Spectrometry · doi:10.1016/s1044-0305(99)00079-3 · Cited by 219
High-resolution mass spectrometry of viral assemblies: Molecular composition and stability of dimorphic hepatitis B virus capsids
Uetrecht, C., Versluis, C., Watts, N. R., Roos, W. H., Wuite, G. J. L., Wingfield, P. T., Steven, A. C., & Heck, A. J. R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800406105 · Cited by 219
Self-citation
Atmospheric pressure ion focusing in a high-field asymmetric waveform ion mobility spectrometer
Guevremont, R., & Purves, R. W. (1999) · Review of Scientific Instruments · doi:10.1063/1.1149599 · Cited by 218
Drift Tube Studies of Atomic Clusters
Jarrold, M. F. (1995) · The Journal of Physical Chemistry · doi:10.1021/j100001a004 · Cited by 208
Protein Folding−Simulation
Daggett, V. (2006) · Chemical Reviews · doi:10.1021/cr0404242 · Cited by 206
Conformations, Unfolding, and Refolding of Apomyoglobin in Vacuum: An Activation Barrier for Gas-Phase Protein Folding
Shelimov, K. B., & Jarrold, M. F. (1997) · Journal of the American Chemical Society · doi:10.1021/ja962914k · Cited by 205
Molecular simulation as an aid to experimentalists
van Gunsteren, W. F., Dolenc, J., & Mark, A. E. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2007.12.007 · Cited by 204
Electrospray ionization mass spectrometry and ion mobility analysis of the 20S proteasome complex
Loo, J. A., Berhane, B., Kaddis, C. S., Wooding, K. M., Xie, Y., Kaufman, S. L., & Chernushevich, I. V. (2005) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2005.02.017 · Cited by 203
Mass spectrometry of macromolecular assemblies: preservation and dissociation
Benesch, J. L., & Robinson, C. V. (2006) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2006.03.009 · Cited by 203
IMS−IMS and IMS−IMS−IMS/MS for Separating Peptide and Protein Fragment Ions
Merenbloom, S. I., Koeniger, S. L., Valentine, S. J., Plasencia, M. D., & Clemmer, D. E. (2006) · Analytical Chemistry · doi:10.1021/ac052208e · Cited by 200
An Ion ``Velocitron''
Cameron, A. E., & Eggers, D. F. (1948) · Review of Scientific Instruments · doi:10.1063/1.1741336 · Cited by 185
Unfolding, Refolding, and Hydration of Proteins in the Gas Phase
Jarrold, M. F. (1999) · Accounts of Chemical Research · doi:10.1021/ar960081x · Cited by 185
Mass Measurements of Increased Accuracy Resolve Heterogeneous Populations of Intact Ribosomes
McKay, A. R., Ruotolo, B. T., Ilag, L. L., & Robinson, C. V. (2006) · Journal of the American Chemical Society · doi:10.1021/ja061468q · Cited by 178
Travelling wave ion mobility mass spectrometry studies of protein structure: biological significance and comparison with X‐ray crystallography and nuclear magnetic resonance spectroscopy measurements
Scarff, C. A., Thalassinos, K., Hilton, G. R., & Scrivens, J. H. (2008) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.3737 · Cited by 178
Design of Helices That Are Stable in Vacuo
Hudgins, R. R., Ratner, M. A., & Jarrold, M. F. (1998) · Journal of the American Chemical Society · doi:10.1021/ja983021q · Cited by 172
Do ionic charges in ESI MS provide useful information on macromolecular structure?
Kaltashov, I. A., & Abzalimov, R. R. (2008) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2008.05.018 · Cited by 170
Process analysis using ion mobility spectrometry
Baumbach, J. I. (2006) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-005-3397-8 · Cited by 170
Gas-Phase Unfolding and Disassembly Reveals Stability Differences in Ligand-Bound Multiprotein Complexes
Hyung, S.-J., Robinson, C. V., & Ruotolo, B. T. (2009) · Chemistry & Biology · doi:10.1016/j.chembiol.2009.02.008 · Cited by 169
Evidence for Many Resolvable Structures within Conformation Types of Electrosprayed Ubiquitin Ions
Koeniger, S. L., Merenbloom, S. I., & Clemmer, D. E. (2006) · The Journal of Physical Chemistry B · doi:10.1021/jp056165h · Cited by 165
High-Resolution Ion Cyclotron Mobility Spectrometry
Merenbloom, S. I., Glaskin, R. S., Henson, Z. B., & Clemmer, D. E. (2009) · Analytical Chemistry · doi:10.1021/ac801880a · Cited by 161
Metabolic profiling by ion mobility mass spectrometry (IMMS)
Dwivedi, P., Wu, P., Klopsch, S. J., Puzon, G. J., Xun, L., & Hill, H. H. (2008) · Metabolomics · doi:10.1007/s11306-007-0093-z · Cited by 160
Sizing large proteins and protein complexes by electrospray ionization mass spectrometry and ion mobility
Kaddis, C. S., Lomeli, S. H., Yin, S., Berhane, B., Apostol, M., Kickhoefer, V., Rome, L. H., & Loo, J. (2007) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2007.02.015 · Cited by 159
Biomolecular structural separations by ion mobility–mass spectrometry
Fenn, L. S., & MCLEAN, J. A. J. (2008) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-008-1951-x · Cited by 156
Toward Plasma Proteome Profiling with Ion Mobility-Mass Spectrometry
Valentine, S. J., Plasencia, M. D., Liu, X., Krishnan, M. R., Naylor, S., Udseth, H. R., Smith, R. D., & Clemmer, D. E. (2006) · Journal of Proteome Research · doi:10.1021/pr060232i · Cited by 156
Gas-Phase Conformations of Synthetic Polymers: Poly(ethylene glycol), Poly(propylene glycol), and Poly(tetramethylene glycol)
Gidden, J. A., Wyttenbach, T., Jackson, A. T., Scrivens, J. H., & Bowers, M. T. (2000) · Journal of the American Chemical Society · doi:10.1021/ja993096+ · Cited by 154
α-Synuclein: Stable compact and extended monomeric structures and pH dependence of dimer formation
Bernstein, S. L., Liu, D., Wyttenbach, T., Bowers, M. T., Lee, J. C., Gray, H. B., & Winkler, J. R. (2004) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2004.08.003 · Cited by 154
Chaperonin Complexes Monitored by Ion Mobility Mass Spectrometry
van Duijn, E., Barendregt, A., Synowsky, S. A., Versluis, C., & Heck, A. J. R. (2009) · Journal of the American Chemical Society · doi:10.1021/ja8055134 · Cited by 152
Self-citation
Resolving and assigning N-linked glycan structural isomers from ovalbumin by IMS-MS
Plasencia, M. D., Isailović, D., Merenbloom, S. I., Mechref, Y. S., & Clemmer, D. E. (2008) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2008.07.020 · Cited by 145
Ion mobility spectrometry—mass spectrometry performance using electrodynamic ion funnels and elevated drift gas pressures
Baker, E. S., Clowers, B. H., Li, F., Tang, K., Tolmachev, A. V., Prior, D. C., Belov, M. E., & Smith, R. D. (2007) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2007.03.031 · Cited by 143
Monitoring copopulated conformational states during protein folding events using electrospray ionization-ion mobility spectrometry-mass spectrometry
Smith, D. P., Giles, K., Bateman, R. H., Radford, S. E., & Ashcroft, A. E. (2007) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2007.09.017 · Cited by 134
Biomolecular folding in vacuo!!!(?)
Wolynes, P. G. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.7.2426 · Cited by 131
Subunit Architecture of Intact Protein Complexes from Mass Spectrometry and Homology Modeling
Taverner, T., Hernández, H., Sharon, M., Ruotolo, B. T., Matak‐Vinković, D., Devos, D. P., Russell, R. B., & Robinson, C. V. (2008) · Accounts of Chemical Research · doi:10.1021/ar700218q · Cited by 131
Evidence for unfolding and refolding of gas-phase cytochrome c ions in a Paul trap
Badman, E. R., Myung, S., & Clemmer, D. E. (2005) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2005.04.013 · Cited by 130
Rapid Identification of Hemoglobin Variants by Electrospray Ionization Mass Spectrometry
Wild, B. J., Green, B. N., Cooper, E., Lalloz, M. R. A., Erten, S., Stephens, A. D., & Layton, D. M. (2001) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.2001.0430 · Cited by 122
Multidimensional separations of ubiquitin conformers in the gas phase: Relating ion cross sections to H/D exchange measurements
Robinson, E. W., & Williams, E. R. (2005) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2005.04.007 · Cited by 120
Fast Two-Dimensional NMR Spectroscopy of High Molecular Weight Protein Assemblies
Amero, C., Schanda, P., Durá, M. A., Ayala, I., Marion, D., Franzetti, B., Brutscher, B., & Boisbouvier, J. (2009) · Journal of the American Chemical Society · doi:10.1021/ja809880p · Cited by 112
Drift Tube-Mass Spectrometer for Studies of Low-Energy Ion-Molecule Reactions
McDaniel, E. W., Martin, D. W., & Barnes, W. S. (1962) · Review of Scientific Instruments · doi:10.1063/1.1717656 · Cited by 111
Stability and Shape of Hepatitis B Virus Capsids In Vacuo
Uetrecht, C., Versluis, C., Watts, N. R. M., Wingfield, P. T., Steven, A. C., & Heck, A. J. R. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200802410 · Cited by 108
Self-citation
Characterizing the Structures and Folding of Free Proteins Using 2-D Gas-Phase Separations: Observation of Multiple Unfolded Conformers
Shvartsburg, A. A., Li, F., Tang, K., & Smith, R. D. (2006) · Analytical Chemistry · doi:10.1021/ac060283z · Cited by 104
Monitoring macromolecular complexes involved in the chaperonin-assisted protein folding cycle by mass spectrometry
van Duijn, E., Bakkes, P. J., Heeren, R. M. A., van den Heuvel, R. H. H., van Heerikhuizen, H., van der Vies, S. M., & Heck, A. J. R. (2005) · Nature Methods · doi:10.1038/nmeth753 · Cited by 104
Self-citation
Collision cross sections of myoglobin and cytochrome c ions with Ne, Ar, and Kr
Chen, Y., Collings, B. A., & Douglascor, D. J. (1997) · Journal of the American Society for Mass Spectrometry · doi:10.1016/s1044-0305(97)00033-0 · Cited by 98
Thermal Unfolding of Unsolvated Cytochrome c: Experiment and Molecular Dynamics Simulations
Mao, Y., Woenckhaus, J., Kolafa, J., Ratner, M. A., & Jarrold, M. F. (1999) · Journal of the American Chemical Society · doi:10.1021/ja980324b · Cited by 96
Investigation of bovine ubiquitin conformers separated by high-field asymmetric waveform ion mobility spectrometry: Cross section measurements using energy-loss experiments with a triple quadrupole mass spectrometer
Purves, R. W., Barnett, D. A., Ells, B., & Guevremont, R. (2000) · Journal of the American Society for Mass Spectrometry · doi:10.1016/s1044-0305(00)00136-7 · Cited by 96
Molecular dynamics simulations of hydrophobic collapse of ubiquitin
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See all 462

Authors: Uetrecht, C., Rose, R. J., van Duijn, E., Lorenzen, K., & Heck, A. J. R.
Venue: Chem. Soc. Rev.
Publisher: Royal Society of Chemistry (RSC)
Published: 2010
Volume: 39
Issue: 5
Pages: 1633-1655
ISSN: 0306-0012 (ISSN-L)
1460-4744
DOI: 10.1039/b914002f
OpenAlex: W2086145691
Cited by: 462
References: 141
FWCI: 1.48
Type: journal article
Language: en
Open access: closed

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Ion mobility mass spectrometry of proteins and proteinassemblies

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