Studying noncovalent protein complexes in aqueous solution with laser desorption mass spectrometry

Wattenberg, Andreas; Sobott, Frank; Barth, Hans-Dieter; Brutschy, Bernhard

doi:10.1016/s1387-3806(00)00261-x

Cited by 54 publications

(26 citation statements)

References 24 publications

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“…However, we should not forget that MALDI is also applied to study these assemblies. Indeed, several recent reports show that MALDI is capable of keeping non-covalent protein interactions intact in the gas-phase vacuum of the mass spectrometer (Kiselar & Downard, 2000;Strupat et al, 2000;Wattenberg et al, 2000;Friess et al, 2002). However, the dried, often acidic, organic matrix is not an ideal environment to keep the proteins under physiologically relevant conditions.…”

Section: Electrospray Ionization Of Biomacromoleculesmentioning

confidence: 99%

Investigation of intact protein complexes by mass spectrometry

Heck

Heuvel

2004

Mass Spectrometry Reviews

550

553

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I. Introduction 00 II. Electrospray Ionization of Biomacromolecules 00 III. Mass Analyzers for Biomacromolecular Mass Spectrometry 00 A. Collisional Cooling and/or Focusing 00 B. Alternative Mass Analyzers 00 IV. Solution‐Phase Properties of Proteins Complexes 00 A. Protein–Protein Interactions 00 B. Cooperativity and Cofactors 00 C. Dynamics of Assembly 00 V. Gas‐Phase Properties of Protein Complexes 00 A. Tandem Mass Spectrometry 00 B. Charge Separation in Protein Dissociation 00 VI. Future Outlook 00 Acknowledgments 00 References 00 Mass spectrometry has grown in recent years to a well‐accepted and increasingly important complementary technique in structural biology. Especially electrospray ionization mass spectrometry is well suited for the detection of non‐covalent protein complexes and their interactions with DNA, RNA, ligands, and cofactors. Over the last decade, significant advances have been made in the ionization and mass analysis techniques, which makes the investigation of even larger and more heterogeneous intact assemblies feasible. These technological developments have paved the way to study intact non‐covalent protein–protein interactions, assembly and disassembly in real time, subunit exchange, cooperativity effects, and effects of cofactors, allowing us a better understanding of proteins in cellular processes. In this review, we describe some of the latest developments and several highlights. © 2004 Wiley Periodicals, Inc., Mass Spec Rev

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Section: Electrospray Ionization Of Biomacromoleculesmentioning

confidence: 99%

Investigation of intact protein complexes by mass spectrometry

Heck

Heuvel

2004

Mass Spectrometry Reviews

550

553

View full text Add to dashboard Cite

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“…The efficiency of separation of ion pairs increases with the dielectric constant of the solvent. The internal energy imparted to LILBID ions has not been quantified yet, but the methods seems promisingly soft: its ability to produce intact non‐covalent complex has been demonstrated (Kleinekofort et al, 1996, 1997; Wattenberg et al, 2000; Wattenberg, Sobott, & Brutschy, 2000).…”

Section: Determination Of Internal Energy In Electrospraymentioning

confidence: 99%

Internal energy and fragmentation of ions produced in electrospray sources

Gabelica

Pauw

2004

Mass Spectrometry Reviews

300

424

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This review addresses the determination of the internal energy of ions produced by electrospray ionization (ESI) sources, and the influence of the internal energy on analyte fragmentation. A control of the analyte internal energy is crucial for several applications of electrospray mass spectrometry, like structural studies, construction of reproducible and exportable spectral libraries, analysis of non-covalent complexes. Sections II and III summarize the Electrospray mechanisms and source design considerations which are relevant to the problem of internal energy, and Section IV gives an overview of the inter-relationships between ion internal energy, reaction time scale, and analyte fragmentation. In these three sections we tried to make the most important theoretical elements understandable by all ESI users, and their understanding requires a minimal background in physical chemistry. We then present the different approaches used to experimentally determine the ion internal energy, as well as various attempts in modeling the internal energy uptake in electrospray sources. Finally, a tentative comparison between electrospray and other ionization sources is made. As the reader will see, although many reports appeared on the subject, the knowledge in the field of internal energy of ions produced by soft ionization sources is still scarce, because of the complexity of the system, and this is what makes this area of research so interesting. The last section presents some perspectives for future research.

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“…There is one other potential technique which may eventually play a role in this context. Brutschy and collaborators have developed a desorption method which they call laser induced liquid beam ionization/desorption mass spectrometry (LILBID-MS) (see Wattenberg et al (2000) and references cited therein). With this method it is possible to desorb solvated ions directly from a liquid.…”

Section: Electrospray and Other Techniques For Mass Spectrometry Of Mmentioning

confidence: 99%

Ultrafast dynamics in isolated molecules and molecular clusters

2006

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During the past decade the understanding of photo-induced ultrafast dynamics in molecular systems has improved at an unforeseen speed and a wealth of detailed insight into the fundamental processes has been obtained. This review summarizes our present knowledge on ultrafast dynamics in isolated molecules and molecular clusters evolving after excitation with femtosecond pulses as studied by pump-probe analysis in real time. Experimental tools and methods as well as theoretical models are described which have been developed to glean information on primary, ultrafast processes in photophysics, photochemistry and photobiology. The relevant processes are explained by way of example-from wave packet dynamics in systems with a few atoms all the way to internal conversion via conical intersections in bio-chromophores. A systematic overview on characteristic systems follows, starting with diatomic and including larger organic molecules as well as various types of molecular clusters, such as micro-solvated chromophore molecules. For conciseness the focus is on molecular systems which remain unperturbed by the laser pulses-apart from the excitation and detection processes as such. Thus, only some aspects of controlling and manipulating molecular reactions by shaped and/or very intense laser pulses are discussed briefly for particularly instructive examples, illustrating the perspectives of this prospering field. The material presented in this review comprises some prototypical examples from earlier pioneering work but emphasizes studies from recent years and covers the most important and latest developments until January 2006.

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Studying noncovalent protein complexes in aqueous solution with laser desorption mass spectrometry

Cited by 54 publications

References 24 publications

Investigation of intact protein complexes by mass spectrometry

Investigation of intact protein complexes by mass spectrometry

Internal energy and fragmentation of ions produced in electrospray sources

Ultrafast dynamics in isolated molecules and molecular clusters

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