Study of Non-covalent Protein Complexes by Electrospray Ionization Mass Spectrometry PDF Download
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Author: Jiangxiao Sun
Publisher:
ISBN:
Category : Electrospray ionization mass spectrometry
Languages : en
Pages : 430
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Author: Jiangxiao Sun
Publisher:
ISBN:
Category : Electrospray ionization mass spectrometry
Languages : en
Pages : 430
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Book Description
Author:
Publisher:
ISBN:
Category :
Languages : en
Pages :
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Author: Lan Liu
Publisher:
ISBN:
Category : Electrospray ionization mass spectrometry
Languages : en
Pages : 338
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Author: Belal Hossain
Publisher:
ISBN:
Category :
Languages : en
Pages : 204
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Author: Yang Kang
Publisher:
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Category :
Languages : en
Pages :
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Author: Yixuan Zhang
Publisher:
ISBN:
Category : Carbohydrates
Languages : en
Pages : 123
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Book Description
This thesis describes the development and application of electrospray ionization mass spectrometry (ESI-MS) based techniques to investigate protein-carbohydrate interactions in vitro. A catch-and-release electrospray ionization mass spectrometry (CaR-ESI-MS) assay was developed for the identification of specific interactions between water-soluble multisubunit proteins and glycosphingolipids (GSL). The assay is of high sensitivity and specificity, and demonstrates the potential for discovering biologically relevant protein-GSL interactions. Collision-induced dissociation (CID) experiments and molecular dynamic simulations were performed to investigate the dissociation pathways of multisubunit protein-ligand complexes in the gas phase. The observation of multiple dissociation pathways suggests that collisional activation of multisubunit protein-ligand complexes in the gas phase is likely to induce significant changes to the nature of the protein-ligand interactions.
Author: Christoph A. Schalley
Publisher: John Wiley & Sons
ISBN: 0470131152
Category : Science
Languages : en
Pages : 593
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Details the many benefits of applying mass spectrometry to supramolecular chemistry Except as a method for the most basic measurements, mass spectrometry (MS) has long been considered incompatible with supramolecular chemistry. Yet, with today's methods, the disconnect between these two fields is not warranted. Mass Spectrometry and Gas-Phase Chemistry of Non-Covalent Complexes provides a convincing look at how modern MS techniques offer supramolecular chemists a powerful investigatory toolset. Bringing the two fields together in an interdisciplinary manner, this reference details the many different topics associated with the study of non-covalent complexes in the gas phase. The text begins with brief introductions to supramolecular chemistry and such relevant mass spectrometric methods as ionization techniques, analyzers, and tandem MS experiments. The coverage continues with: How the analyte's transition into the gas phase changes covalent bonding How limitations and pitfalls in analytical methods may produce data misinterpretations Artificial supramolecular aggregates and their examination Biomolecules, their complexes, and their examination After the general remarks making up the first section of the book, the following sections describe specific experimental procedures and are illustrated with numerous examples and short tutorials. Detailed citations end each chapter. Mass spectrometrists, supramolecular chemists, students in these fields, and interested readers from other disciplines involving the study of non-covalent bonds will all value Mass Spectrometry and Gas-Phase Chemistry of Non-Covalent Complexes as an innovative and practical resource.
Author: Jiangjiang Liu
Publisher:
ISBN:
Category :
Languages : en
Pages : 352
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Since the emergence of electrospray ionization (ESI) mass spectrometry (MS) as a tool for protein structural studies, this area has experienced tremendous growth. ESI-MS is highly sensitive, and it allows the analysis of biological systems ranging in size from a few atoms to large multi-protein complexes. This work aims to solve questions in protein structural biology by using ESI-MS in conjunction with other techniques. We initially apply ESI-MS for studying the monomeric protein cytochrome c (Chapter 2). The physical reasons underlying the irreversible thermal denaturation of this protein remain controversial. By utilizing deconvoluted charge state distributions, oxidative modifications were found to be the major reason underlying the observed behavior. The positions of individual oxidation sites were identified by LC-MS/MS-based tryptic peptide mapping. Chapter 3 and 4 focus on noncovalent protein complexes. ESI allows the transfer of multi-protein complexes into the gas phase, thereby providing a simple approach for monitoring the stoichiometry of these assemblies by MS. It remains somewhat unclear, however, in how far this approach is suitable for measuring binding affinities. We demonstrate that the settings used for rf-only quadrupoles in the ion path are a key factor for ensuring uniform transmission behavior, which is a prerequisite for meaningful Kd measurements. Overall, our data support the viability of the direct ESI-MS approach for determining binding affinities of protein-protein complexes in solution. Having established suitable conditions for the analysis of noncovalent protein complexes, ESI-MS is applied for monitoring the folding and assembly of hemoglobin (Hb). The native structure of this protein comprises four heme-bound subunits. Hb represents an important model system for exploring coupled folding/binding reactions, an area that remains difficult to tackle experimentally. We demonstrate that efficient Hb refolding depends on the heme ligation status. Only under properly optimized conditions is it possible to return denatured Hb to its tetrameric native state with high yield. ESI-MS allows the observation of on-pathway and off-pathway intermediates that become populated during this highly complex self-assembly process. In summary, this work demonstrates that ESI-MS is a highly versatile tool for addressing questions at the interface of chemistry and structural biology.
Author: Esther Caroline Kempen
Publisher:
ISBN:
Category : Mass spectrometry
Languages : en
Pages : 306
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Author:
Publisher:
ISBN:
Category :
Languages : en
Pages : 436
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