PROBING GAS-PHASE PEPTIDE STRUCTURE AND PROTEIN-PROTEIN INTERACTIONS USING MASS SPECTROMETRIC TECHNIQUES.

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ISBN 13 :
Total Pages : 640 pages
Book Rating : 4.:/5 (659 download)

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Book Synopsis PROBING GAS-PHASE PEPTIDE STRUCTURE AND PROTEIN-PROTEIN INTERACTIONS USING MASS SPECTROMETRIC TECHNIQUES. by :

Download or read book PROBING GAS-PHASE PEPTIDE STRUCTURE AND PROTEIN-PROTEIN INTERACTIONS USING MASS SPECTROMETRIC TECHNIQUES. written by and published by . This book was released on 2009 with total page 640 pages. Available in PDF, EPUB and Kindle. Book excerpt: Presented in this dissertation are studies on the gas-phase structural features of peptides and peptide fragment ions using mass spectrometry (MS), hydrogen/deuterium (H/D) exchange, infrared multiphoton dissociation (IRMPD) spectroscopy, and computational modeling. Additional studies are presented on the mechanism of hydrogen/deuterium exchange using a model amino acid system. The application of chemical cross-linking to investigate the interaction between two proteins, LexA and RecA, is also presented. Gas-phase structural features can be probed using a number of techniques, and several of the studies presented in this dissertation involve the use of gas-phase H/D exchange. Although the basic mechanism for exchange has been determined, the factors that affect the rate and extent of exchange are not well understood. A computational modeling study of the exchange behavior of asparagine and its methyl ester demonstrated that exchange will occur preferentially at sites of more similar basicity. The distinctive exchange behavior of a model histidine-containing pentapeptide, HAAAA, prompted further studies into the structural features that result in five fast exchanging hydrogens and one slower exchange. Peptide analogues were used to identify the sites of exchange, and IRMPD spectroscopy combined with computational modeling indicated that exchange may occur because interaction with water at those sites results in lower energy structures compared to the other sites. Structural studies were also performed to determine whether the b2+ion from HAAAA is an oxazolone or diketopiperazine. The IRMPD spectrum showed bands that matched both a diketopiperazine and an oxazolone structure. H/D exchange and fragmentation studies further supported the presence of a mixture of species. Protein-protein interactions perform a vital role in regulating cellular processes. Despite extensive mutational analysis, the binding interaction between LexA and RecA, two proteins involved in the SOS response, is unclear. Chemical cross-linking experiments were undertaken to help target future mutational studies, and these studies identified two possible interactions. The first potential binding interaction is located in the cleft of RecA, and the second interaction may be caused by a LexA dimer binding across the RecA helical groove. The presence of two different binding interactions suggests that LexA may have redundant binding modes for RecA interaction.

Mass Spectrometry Analysis for Protein-Protein Interactions and Dynamics

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Publisher : John Wiley & Sons
ISBN 13 : 0470258861
Total Pages : 325 pages
Book Rating : 4.4/5 (72 download)

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Book Synopsis Mass Spectrometry Analysis for Protein-Protein Interactions and Dynamics by : M. Chance

Download or read book Mass Spectrometry Analysis for Protein-Protein Interactions and Dynamics written by M. Chance and published by John Wiley & Sons. This book was released on 2008-09-22 with total page 325 pages. Available in PDF, EPUB and Kindle. Book excerpt: Presents a wide variety of mass spectrometry methods used to explore structural mechanisms, protein dynamics and interactions between proteins. Preliminary chapters cover mass spectrometry methods for examining proteins and are then followed by chapters devoted to presenting very practical, how-to methods in a detailed way. Includes footprinting and plistex specifically, setting this book apart from the competition.

Mass Spectrometry of Protein Interactions

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Publisher : John Wiley & Sons
ISBN 13 : 047014632X
Total Pages : 153 pages
Book Rating : 4.4/5 (71 download)

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Book Synopsis Mass Spectrometry of Protein Interactions by : Kevin Downard

Download or read book Mass Spectrometry of Protein Interactions written by Kevin Downard and published by John Wiley & Sons. This book was released on 2007-08-24 with total page 153 pages. Available in PDF, EPUB and Kindle. Book excerpt: The authoritative guide to analyzing protein interactions by mass spectrometry Mass spectrometry (MS) is playing an increasingly important role in the study of protein interactions. Mass Spectrometry of Protein Interactionspresents timely and definitive discussions of the diverse range of approaches for studying protein interactions by mass spectrometry with an extensive set of references to the primary literature. Each chapter is written by authors or teams of authors who are international authorities in their fields. This leading reference text: * Discusses the direct detection of protein interactions through electrospray ionization (ESI-MS); ion mobility analysis; and matrix-assisted laser desorption/ionization (MALDI-MS) * Covers the indirect analysis of protein interactions through hydrogen-deuterium exchange (HX-MS); limited proteolysis; cross-linking; and radial probe (RP-MS) * Guides researchers in the use of mass spectrometry in structural biology, biochemistry, and protein science to map and define the huge number and diversity of protein interactions * Reviews the latest discoveries and applications and addresses new and ongoing challenges This is a comprehensive reference for researchers in academia and industry engaged in studies of protein interactions and an excellent text for graduate and postgraduate students.

Protein and Peptide Analysis by Mass Spectrometry

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Publisher : Springer Science & Business Media
ISBN 13 :
Total Pages : 368 pages
Book Rating : 4.3/5 (91 download)

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Book Synopsis Protein and Peptide Analysis by Mass Spectrometry by : J. R. Chapman

Download or read book Protein and Peptide Analysis by Mass Spectrometry written by J. R. Chapman and published by Springer Science & Business Media. This book was released on 1996-08-19 with total page 368 pages. Available in PDF, EPUB and Kindle. Book excerpt: Leading practitioners authoritatively describe the newest and most effective spectrometric techniques for the analysis of proteins and peptides. The areas covered range from the elucidation of primary and secondary protein structure and the rapid identification of proteins using database techniques to methods for sequencing, as well as methods for the quantitative determination of peptides. Other chapters provide detailed information on the analysis of glycoproteins and glycopeptides and on the use of mass spectrometry to probe the interactions of proteins, both covalent and noncovalent.

Mass Spectrometry in Biophysics

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Publisher : John Wiley & Sons
ISBN 13 : 0471705160
Total Pages : 320 pages
Book Rating : 4.4/5 (717 download)

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Book Synopsis Mass Spectrometry in Biophysics by : Igor A. Kaltashov

Download or read book Mass Spectrometry in Biophysics written by Igor A. Kaltashov and published by John Wiley & Sons. This book was released on 2005-05-06 with total page 320 pages. Available in PDF, EPUB and Kindle. Book excerpt: The first systematic summary of biophysical mass spectrometrytechniques Recent advances in mass spectrometry (MS) have pushed the frontiersof analytical chemistry into the biophysical laboratory. As aresult, the biophysical community's acceptance of MS-based methods,used to study protein higher-order structure and dynamics, hasaccelerated the expansion of biophysical MS. Despite this growing trend, until now no single text has presentedthe full array of MS-based experimental techniques and strategiesfor biophysics. Mass Spectrometry in Biophysics expertly closesthis gap in the literature. Covering the theoretical background and technical aspects of eachmethod, this much-needed reference offers an unparalleled overviewof the current state of biophysical MS. Mass Spectrometry inBiophysics begins with a helpful discussion of general biophysicalconcepts and MS-related techniques. Subsequent chaptersaddress: * Modern spectrometric hardware * High-order structure and dynamics as probed by various MS-basedmethods * Techniques used to study structure and behavior of non-nativeprotein states that become populated under denaturingconditions * Kinetic aspects of protein folding and enzyme catalysis * MS-based methods used to extract quantitative information onprotein-ligand interactions * Relation of MS-based techniques to other experimental tools * Biomolecular properties in the gas phase Fully referenced and containing a helpful appendix on the physicsof electrospray mass spectrometry, Mass Spectrometry in Biophysicsalso offers a compelling look at the current challenges facingbiomolecular MS and the potential applications that will likelyshape its future.

Characterization of Peptides, Proteins, and Protein Complexes Using Infrared Multiphoton Dissociation Spectroscopy, Ion Mobility Spectrometry, and Surface-induced Dissociation Mass Spectrometry

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ISBN 13 :
Total Pages : 210 pages
Book Rating : 4.:/5 (13 download)

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Book Synopsis Characterization of Peptides, Proteins, and Protein Complexes Using Infrared Multiphoton Dissociation Spectroscopy, Ion Mobility Spectrometry, and Surface-induced Dissociation Mass Spectrometry by : Erin M. Panczyk

Download or read book Characterization of Peptides, Proteins, and Protein Complexes Using Infrared Multiphoton Dissociation Spectroscopy, Ion Mobility Spectrometry, and Surface-induced Dissociation Mass Spectrometry written by Erin M. Panczyk and published by . This book was released on 2021 with total page 210 pages. Available in PDF, EPUB and Kindle. Book excerpt: Mass spectrometry-based techniques have emerged as powerful analytical tools to investigate the structure of proteins from the primary to quaternary levels. The advancement of mass spectrometry instrumentation and methods has allowed researchers to go beyond just measuring an analyte’s mass-to-charge ratio, but to also probe gas-phase dissociation behaviors and conformations of peptides, proteins, and protein complexes. The primary structure of a protein refers to the linear sequence of amino acids linked together via peptide bonds. The presence, and the order, of specific amino acids in a peptide can strongly influence how a peptide fragments in the gas-phase. Particular amino acids can direct where along the peptide backbone fragmentation is favored and the structure of the fragment ions formed. One method for probing the structure of peptide fragment ions is infrared multiphoton dissociation (IRMPD) mass spectrometry coupled with theoretical quantum chemical calculations. This approach is used to investigate the role of peptide bond conformation on the structure of b2+ fragment ions formed from proline and dimethylproline-containing peptides (Chapter 3). Additionally, IRMPD is used to study the fragmentation patterns of proline containing pentapeptides into b3+ ions (Chapter 4). Native mass spectrometry (nMS) analyzes the intact structures of proteins and protein complexes and offers complementary information to traditional biophysical methods, such as NMR or cryo-EM. Tandem mass spectrometry, specifically surface-induced dissociation (SID), provides information on protein complex connectivity, stoichiometry, and gas-phase structural rearrangement. SID is utilized to monitor deviation from native structure for protein complexes generated from submicrometer nanoelectrospray capillaries (Chapter 5), as well as to provide insight into connectivity of protein complexes selected by trapped ion mobility spectrometry (Chapter 6). In addition to SID, ion mobility spectrometry provides information on the gas-phase shape or conformation of biomolecules. Here, ion mobility spectrometry is utilized to separate multiple conformers of proline-containing peptides (Chapter 3), compare the collision cross sections of protein complexes generated from submicrometer and micrometer sized nanoelectrospray capillaries (Chapter 5), and select protein complexes and isomeric peptides prior to dissociation on an ultrahigh resolution mass spectrometry platform (Chapter 6). Finally, the development and optimization of Trapped Ion Mobility Spectrometry (TIMS) for native mass spectrometry applications is applied to the widely available timsTOF Pro mass spectrometry platform to promote the dissemination of native ion mobility technology.

Mass Spectrometry in Structural Biology and Biophysics

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Publisher : John Wiley & Sons
ISBN 13 : 0470937793
Total Pages : 312 pages
Book Rating : 4.4/5 (79 download)

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Book Synopsis Mass Spectrometry in Structural Biology and Biophysics by : Igor A. Kaltashov

Download or read book Mass Spectrometry in Structural Biology and Biophysics written by Igor A. Kaltashov and published by John Wiley & Sons. This book was released on 2012-04-03 with total page 312 pages. Available in PDF, EPUB and Kindle. Book excerpt: The definitive guide to mass spectrometry techniques in biology and biophysics The use of mass spectrometry (MS) to study the architecture and dynamics of proteins is increasingly common within the biophysical community, and Mass Spectrometry in Structural Biology and Biophysics: Architecture, Dynamics, and Interaction of Biomolecules, Second Edition provides readers with detailed, systematic coverage of the current state of the art. Offering an unrivalled overview of modern MS-based armamentarium that can be used to solve the most challenging problems in biophysics, structural biology, and biopharmaceuticals, the book is a practical guide to understanding the role of MS techniques in biophysical research. Designed to meet the needs of both academic and industrial researchers, it makes mass spectrometry accessible to professionals in a range of fields, including biopharmaceuticals. This new edition has been significantly expanded and updated to include the most recent experimental methodologies and techniques, MS applications in biophysics and structural biology, methods for studying higher order structure and dynamics of proteins, an examination of other biopolymers and synthetic polymers, such as nucleic acids and oligosaccharides, and much more. Featuring high-quality illustrations that illuminate the concepts described in the text, as well as extensive references that enable the reader to pursue further study, Mass Spectrometry in Structural Biology and Biophysics is an indispensable resource for researchers and graduate students working in biophysics, structural biology, protein chemistry, and related fields.

Mass Spectrometry of Proteins and Peptides

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Publisher : Springer Science & Business Media
ISBN 13 : 1592590454
Total Pages : 539 pages
Book Rating : 4.5/5 (925 download)

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Book Synopsis Mass Spectrometry of Proteins and Peptides by : John R. Chapman

Download or read book Mass Spectrometry of Proteins and Peptides written by John R. Chapman and published by Springer Science & Business Media. This book was released on 2008-02-05 with total page 539 pages. Available in PDF, EPUB and Kindle. Book excerpt: Little more than three years down the line and I am already writing the Preface to a second volume to follow Protein and Peptide Analysis by Mass . What has happened in between these times to make this second venture worthwhile? New types of mass spectrometric instrumentation have appeared so that new techniques have become possible and existing techniques have become much more feasible. More particularly, however, the newer ionization te- niques, introduced for the analysis of high molecular weight materials, have now been thoroughly used and studied. As a result, there has been an en- mous improvement in the associated sample handling technology so that these methods are now routinely applied to much smaller sample amounts as well as to more intractable samples. Again, this particular community of mass spectrometry users has both increased in number and diversified. And, riding this wave of acceptance, leaders in the field have set their sights on more complex problems: molecular interaction, ion structures, quantitation, and kinetics are just a few of the newer areas reported in Mass Spectrometry of Proteins and Peptides. As with the first volume, one purpose of this collection, Mass Spectr- etry of Proteins and Peptides, is to show the reader what can be done by the application of mass spectrometry, and perhaps even to encourage the reader to venture down new paths.

Hydrogen Exchange Mass Spectrometry of Proteins

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Publisher : John Wiley & Sons
ISBN 13 : 1118616499
Total Pages : 422 pages
Book Rating : 4.1/5 (186 download)

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Book Synopsis Hydrogen Exchange Mass Spectrometry of Proteins by : David D. Weis

Download or read book Hydrogen Exchange Mass Spectrometry of Proteins written by David D. Weis and published by John Wiley & Sons. This book was released on 2016-03-21 with total page 422 pages. Available in PDF, EPUB and Kindle. Book excerpt: Hydrogen exchange mass spectrometry is widely recognized for its ability to probe the structure and dynamics of proteins. The application of this technique is becoming widespread due to its versatility for providing structural information about challenging biological macromolecules such as antibodies, flexible proteins and glycoproteins. Although the technique has been around for 25 years, this is the first definitive book devoted entirely to the topic. Hydrogen Exchange Mass Spectrometry of Proteins: Fundamentals, Methods and Applications brings into one comprehensive volume the theory, instrumentation and applications of Hydrogen Exchange Mass Spectrometry (HX-MS) - a technique relevant to bioanalytical chemistry, protein science and pharmaceuticals. The book provides a solid foundation in the basics of the technique and data interpretation to inform readers of current research in the method, and provides illustrative examples of its use in bio- and pharmaceutical chemistry and biophysics In-depth chapters on the fundamental theory of hydrogen exchange, and tutorial chapters on measurement and data analysis provide the essential background for those ready to adopt HX-MS. Expert users may advance their current understanding through chapters on methods including membrane protein analysis, alternative proteases, millisecond hydrogen exchange, top-down mass spectrometry, histidine exchange and method validation. All readers can explore the diversity of HX-MS applications in areas such as ligand binding, membrane proteins, drug discovery, therapeutic protein formulation, biocomparability, and intrinsically disordered proteins.

Mass Spectrometry-Based Chemical Proteomics

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Publisher : John Wiley & Sons
ISBN 13 : 1118970217
Total Pages : 448 pages
Book Rating : 4.1/5 (189 download)

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Book Synopsis Mass Spectrometry-Based Chemical Proteomics by : W. Andy Tao

Download or read book Mass Spectrometry-Based Chemical Proteomics written by W. Andy Tao and published by John Wiley & Sons. This book was released on 2019-07-10 with total page 448 pages. Available in PDF, EPUB and Kindle. Book excerpt: PROVIDES STRATEGIES AND CONCEPTS FOR UNDERSTANDING CHEMICAL PROTEOMICS, AND ANALYZING PROTEIN FUNCTIONS, MODIFICATIONS, AND INTERACTIONS—EMPHASIZING MASS SPECTROMETRY THROUGHOUT Covering mass spectrometry for chemical proteomics, this book helps readers understand analytical strategies behind protein functions, their modifications and interactions, and applications in drug discovery. It provides a basic overview and presents concepts in chemical proteomics through three angles: Strategies, Technical Advances, and Applications. Chapters cover those many technical advances and applications in drug discovery, from target identification to validation and potential treatments. The first section of Mass Spectrometry-Based Chemical Proteomics starts by reviewing basic methods and recent advances in mass spectrometry for proteomics, including shotgun proteomics, quantitative proteomics, and data analyses. The next section covers a variety of techniques and strategies coupling chemical probes to MS-based proteomics to provide functional insights into the proteome. In the last section, it focuses on using chemical strategies to study protein post-translational modifications and high-order structures. Summarizes chemical proteomics, up-to-date concepts, analysis, and target validation Covers fundamentals and strategies, including the profiling of enzyme activities and protein-drug interactions Explains technical advances in the field and describes on shotgun proteomics, quantitative proteomics, and corresponding methods of software and database usage for proteomics Includes a wide variety of applications in drug discovery, from kinase inhibitors and intracellular drug targets to the chemoproteomics analysis of natural products Addresses an important tool in small molecule drug discovery, appealing to both academia and the pharmaceutical industry Mass Spectrometry-Based Chemical Proteomics is an excellent source of information for readers in both academia and industry in a variety of fields, including pharmaceutical sciences, drug discovery, molecular biology, bioinformatics, and analytical sciences.

Mass Spectrometry-based Strategies for Protein Biophysics

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ISBN 13 :
Total Pages : 193 pages
Book Rating : 4.:/5 (973 download)

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Book Synopsis Mass Spectrometry-based Strategies for Protein Biophysics by : Yining Huang

Download or read book Mass Spectrometry-based Strategies for Protein Biophysics written by Yining Huang and published by . This book was released on 2016 with total page 193 pages. Available in PDF, EPUB and Kindle. Book excerpt: Mass spectrometry (MS) is an essential tool to study proteins whose structures are of great importance in biological systems. The primary structures of proteins can be determined by the powerful sequencing capabilities of MS. The recent advancements in instrumentation and methodology have made MS increasingly valuable in probing secondary, tertiary and quaternary structures, as well as binding strength, interfaces and in solution dynamics of proteins and protein complexes. Various protein footprinting techniques, including hydrogen-deuterium exchange (HDX) and fast photochemical oxidation of proteins (FPOP), encode structural information onto the protein molecule in different forms of modifications, and then MS is utilized to interpret the mass shifts resulted from modifications and extract the structural information. Protein footprinting coupled with bottom-up proteomics, which utilizes front-end LC separation and tandem mass spectrometry, has gained a solid ground in protein biophysics. On the other hand, opportunities emerge as native MS, ion-mobility separation, gas-phase activation and fragmentation techniques allow new approaches to be developed. In the first part of this dissertation, we describe epitope mapping of three malaria antigens (Plasmodium vivax Duffy binding protein in Chapter 2, Plasmodium vivax and falciparum cell-traversal protein for ookinetes and sporozoites in Chapter 6) and one flavivirus antigen (West Nile virus envelope protein domain III (DIII) in Chapter 4) by HDX in combination with bottom-up MS. We also report epitope mapping of DIII antigen by FPOP (Chapter 5). Challenged by highly disulfide-linked antigens, sample complexity and discontinuous epitopes with only a few residues each, we implemented immunoprecipitation, non-canonical quenching and digestion protocols to achieve complete sequence coverage and map the epitopes with high confidence and spatial resolution. In the second part (Chapter 3), we describe the usage of native MS and ion mobility to characterize antigen-antibody complexes formed by the Duffy binding protein antigen with various antibodies targeting different epitopes. The last part (chapter 7 and 8) describes the development an on-line HDX, native-spray platform in conjunction with top-down MS. The strategy is validated by determining the amide hydrogen exchange rates of a model peptide at the residue level. With evidence for adequate mixing efficiency, high sequence coverage, low hydrogen scrambling and capable data analysis, we applied the platform to study solution-phase amyloid beta 1-40 monomer structure by continuous-labeling and monitoring exchange kinetics and to probe the dimerization interfaces of human insulin by pulse-labeling experiment. These seven studies demonstrate the applications of the mature bottom-up and promising top-down MS on characterizing protein conformation and protein-protein interactions.

Protein and Peptide Mass Spectrometry in Drug Discovery

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Publisher : John Wiley & Sons
ISBN 13 : 1118116542
Total Pages : 484 pages
Book Rating : 4.1/5 (181 download)

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Book Synopsis Protein and Peptide Mass Spectrometry in Drug Discovery by : Michael L. Gross

Download or read book Protein and Peptide Mass Spectrometry in Drug Discovery written by Michael L. Gross and published by John Wiley & Sons. This book was released on 2011-09-26 with total page 484 pages. Available in PDF, EPUB and Kindle. Book excerpt: The book that highlights mass spectrometry and its application in characterizing proteins and peptides in drug discovery An instrumental analytical method for quantifying the mass and characterization of various samples from small molecules to large proteins, mass spectrometry (MS) has become one of the most widely used techniques for studying proteins and peptides over the last decade. Bringing together the work of experts in academia and industry, Protein and Peptide Mass Spectrometry in Drug Discovery highlights current analytical approaches, industry practices, and modern strategies for the characterization of both peptides and proteins in drug discovery. Illustrating the critical role MS technology plays in characterizing target proteins and protein products, the methods used, ion mobility, and the use of microwave radiation to speed proteolysis, the book also covers important emerging applications for neuroproteomics and antigenic peptides. Placing an emphasis on the pharmaceutical industry, the book stresses practice and applications, presenting real-world examples covering the most recent advances in mass spectrometry, and providing an invaluable resource for pharmaceutical scientists in industry and academia, analytical and bioanalytical chemists, and researchers in protein science and proteomics.

Radically Defining Protein Behavior in the Gas-phase

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Publisher :
ISBN 13 : 9780438897878
Total Pages : 107 pages
Book Rating : 4.8/5 (978 download)

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Book Synopsis Radically Defining Protein Behavior in the Gas-phase by : James Garrett Bonner

Download or read book Radically Defining Protein Behavior in the Gas-phase written by James Garrett Bonner and published by . This book was released on 2018 with total page 107 pages. Available in PDF, EPUB and Kindle. Book excerpt: Specific factors scrutinized herein include a detailed understanding of participating electrostatic interactions within gas-phase peptides and proteins, as these are the most influential factors for the structures in the absence of intermolecular interactions. The exquisite precision afforded by action excitation energy transfer paired with molecular dynamics is used to probe local ion-dipole and ion-ion behavior in the absence of solvent versus partial solvation. Utilizing a newly developed technique termed photoelectron transfer dissociation, the prevalence of gaseous zwitterions are investigated. This particular coulombic interaction was chosen due to important structural implications being tied to their existence and the fact that little is currently known about their propensity to exist in the gas-phase. Efforts are also made to facilitate crosslinking analysis used for structural elucidation by incorporating 213 nm UVPD into the MS/MS workflow. Crosslink-specific fragmentation produces reporter ions able to drastically reduce search space allowing for confident identification and further insights into molecular structure. These and other experiments serve to better our understanding of protein structure and its stability outside of a native context.

Hydrogen Deuterium Exchange Mass Spectrometry for Protein-protein Interaction and Structural Dynamics

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ISBN 13 :
Total Pages : 159 pages
Book Rating : 4.:/5 (87 download)

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Book Synopsis Hydrogen Deuterium Exchange Mass Spectrometry for Protein-protein Interaction and Structural Dynamics by : Harsimran Singh

Download or read book Hydrogen Deuterium Exchange Mass Spectrometry for Protein-protein Interaction and Structural Dynamics written by Harsimran Singh and published by . This book was released on 2013 with total page 159 pages. Available in PDF, EPUB and Kindle. Book excerpt: Hydrogen deuterium exchange mass spectrometry has emerged as an important technique to probe protein structure and conformational dynamics. The rate of exchange of hydrogen with deuterium by the peptide backbone is dependent on the solvent accessibility, extent of hydrogen bonding in secondary structural elements and protein dynamics. The extent and the rate of deuterium incorporation are affected by changes in protein structure, interaction with ligand, protein-protein interaction and environmental factors such as pH and temperature. These conformational changes can be global and/or local. The increase in the mass is used to localize the deuterium incorporation after pepsin digestion of the protein and analysis by electrospray ionization mass spectrometry. In this dissertation traditional HDX-MS and a new deuterium trapping assay were used to probe the interaction sites between E. coli cysteine desulfurase SufS and acceptor protein SufE. SufS and SufE form an important part of the SUF pathway, essential for the biosynthesis of Fe-S clusters under oxidative stress and iron depletion conditions. In addition, SufE is known to stimulate SufS cysteine desulfurase activity, but the mechanism is unknown. The HDX-MS results show that the regions affected by the SufS-SufE interaction are dependent on the catalytic intermediate states of the two proteins. HDX-MS was also used to probe the conformational changes resulting upon persulfuration of SufS of Cys364 in the active site. The persulfuration of SufS not only affected regions in the active site cavity, but also had other conformational changes in more distal regions. Based on our findings a model for the interaction SufS and SufE was proposed. A mechanism for the enhancement of SufS cysteine desulfurase activity upon interaction with SufE was also postulated. In all this work demonstrates that hydrogen deuterium exchange mass spectrometry and the deuterium trapping methodology optimized for this system can be easily and effectively used to study the protein-protein interactions and the accompanying changes in structural dynamics for other proteins. Deuterium trapping was demonstrated to be fast, sensitive and reliable method to deduce the changes in solvent accessibility between two or more states of a protein. Both techniques can easily be applied to large number of protein complexes to determine the regions of interaction as well as gain mechanistic information not available through traditional methods such as X-ray crystallography and NMR.

Advancing Chemical Cross-linking Mass Spectrometry for Protein Structure and Interaction Analysis

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Publisher :
ISBN 13 :
Total Pages : 0 pages
Book Rating : 4.5/5 (16 download)

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Book Synopsis Advancing Chemical Cross-linking Mass Spectrometry for Protein Structure and Interaction Analysis by : Bingqing Zhao (Bioanalytical chemist)

Download or read book Advancing Chemical Cross-linking Mass Spectrometry for Protein Structure and Interaction Analysis written by Bingqing Zhao (Bioanalytical chemist) and published by . This book was released on 2021 with total page 0 pages. Available in PDF, EPUB and Kindle. Book excerpt: Chemical cross-linking mass spectrometry elucidates protein structures and protein-protein interactions by establishing distance constraints between residues pairs. Interpreting the mass spectra of covalently linked peptide pairs is more challenging than identifying peptides in proteomics. This dissertation presents improvements in methodology for identifying cross-linked peptides and their application to probing protein interacting surfaces.

Improved Cross-linking Mass Spectrometry Algorithms for Probing Protein Structures and Interactions

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ISBN 13 :
Total Pages : 0 pages
Book Rating : 4.:/5 (14 download)

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Book Synopsis Improved Cross-linking Mass Spectrometry Algorithms for Probing Protein Structures and Interactions by : Eugen Netz

Download or read book Improved Cross-linking Mass Spectrometry Algorithms for Probing Protein Structures and Interactions written by Eugen Netz and published by . This book was released on 2023 with total page 0 pages. Available in PDF, EPUB and Kindle. Book excerpt: Proteins are the most active molecules in living bodies. They catalyze chemical reactions, provide structural support for cells and allow organisms to move. Their function is intrinsically linked to their folded structure. Resolving the structures of proteins and protein complexes is crucial for our understanding of basic biological processes and diseases. Cross-Linking Mass Spectrometry (XL-MS) is a method to gain structural insights into protein complexes. The field of XL-MS data analysis software is not yet as established as many other methods in proteomics. XL-MS analysis software has significant room for improvement in terms of sensitivity, efficiency and standardization of file formats and workflows to facilitate interoperability and reproducibility. In this thesis we present a new XL-MS search engine, OpenPepXL. We develop an algorithm that scores all candidate cross-linked peptide pairs and is efficient enough to be used on a standard desktop PC for most applications. OpenPepXL supports the standardized XL-MS identification file format defined as a part of the MzIdentML 1.2 specifications that were developed in collaboration with the Proteomics Standards Initiative. We benchmark OpenPepXL against other state-of-the-art XL-MS identification tools on multiple datasets that allow cross-link validation through structures or other means. We show that our exhaustive approach, although not the quickest one, is superior in sensitivity to other tools. We suggest this is due to some tools improving their processing time by discarding too many candidates in early steps of the data analysis. We apply XL-MS analysis with OpenPepXL to multiple protein complexes related to meiosis and the type III secretion system. The first project involved several proteins with unknown structures, some of which are expected to be at least partially intrinsically disordered and therefore difficult to investigate using most traditional structural research methods. Unfortunately, we could not find cross-links between the interaction sites we were interested in the most, but we were able to identify many others in these complexes and gained some structural insights. In the second project we used the photo-cross-linking amino acid pBpa to test very specific hypotheses about interactions within the type III secretion system. We were not able to gain any new structural information yet. However, we could confirm that this is a viable approach. It is possible to identify cross-links between a pBpa residue incorporated into a protein sequence and a residue it cross-links to on a residue level resolution.

Probing Protein-protein Interactions by Mass Spectrometry

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ISBN 13 :
Total Pages : 147 pages
Book Rating : 4.:/5 (73 download)

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Book Synopsis Probing Protein-protein Interactions by Mass Spectrometry by : Tatiana Pimenova

Download or read book Probing Protein-protein Interactions by Mass Spectrometry written by Tatiana Pimenova and published by . This book was released on 2009 with total page 147 pages. Available in PDF, EPUB and Kindle. Book excerpt: