[PDF] Mass Spectrometry Analysis Reveals Sequence And Higher Order Structure Information For Proteins And Protein Complexes eBook

Author : Carter Lantz
Publisher :
Page : 0 pages
File Size : 28,58 MB
Release : 2022
Category :
ISBN :

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Mass spectrometry (MS) has been found to be a useful technique for the study of various compounds. Fundamentally, MS is a way to measure the masses of compounds for the purpose of identifying and quantifying those compounds. Protein mass spectrometry, where proteins are the analyte of interest, has been found to return relevant information on those proteins including the mass, the identity and location of modifications, and even aspects of protein higher-order structure. The work here aims to develop mass spectrometry methods for the study of proteins and to use those methods to investigate amyloid proteins common in neurodegenerative diseases. Herein, it is described how ClipsMS, a program that assigns internal fragments resulting from top-down mass spectrometry (TD-MS), can be utilized to increase the sequence coverage of proteins and locate modifications. This work also illustrates how native TD-MS of large protein complexes with high-energy C-trap dissociation (HCD) can release covalent fragments that reveal aspects of higher-order structure. Furthermore, it is described how TD-MS of proteins with electron capture dissociation (ECD) on an orbitrap-based mass spectrometer can return relevant information on proteins including sequence information, the location of modifications, and higher-order structure information on protein complexes. In this work, MS techniques were also utilized to characterize neurodegenerative disease protein monomers and oligomers. The research conducted reveals the location of phosphorylation sites on commonly phosphorylated amyloid proteins and that phosphorylation compacts the gas-phase structure of those proteins. It is possible that structure alteration due to phosphorylation could modulate the aggregation potential of amyloid proteins. In addition, it was found that CLR01, a molecular tweezer compound that has been found to inhibit amyloid protein aggregation, directly interacts with the N-terminus of multiple proteoforms of the amyloid protein [alpha]-synuclein and that the molecule compacts the gas-phase structure of the protein. It is possible that compaction of the N-terminal region of [alpha]-synuclein by CLR01 could prevent monomers from interacting with one another and forming oligomers and fibrils of the protein. Lastly, MS was utilized to determine size information and aggregation interface information for various amyloid protein oligomers. Characterization of these small aggregates could provide information on how they become toxic in brain neurons. The data presented here aims to further mass spectrometry methods for the characterization of proteins and to use those methods to reveal protein aggregation mechanisms and discover possible therapies for neurodegenerative diseases.

Author : M. Chance
Publisher : John Wiley & Sons
Page : 325 pages
File Size : 26,77 MB
Release : 2008-09-22
Category : Science
ISBN : 0470258861

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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.

Author : John R. Chapman
Publisher : Springer Science & Business Media
Page : 539 pages
File Size : 22,20 MB
Release : 2008-02-05
Category : Science
ISBN : 1592590454

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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.

Author : Roland Kellner
Publisher : John Wiley & Sons
Page : 346 pages
File Size : 41,47 MB
Release : 2008-09-26
Category : Science
ISBN : 3527613978

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Proteomics - the analysis of the whole set of proteins and their functions in a cell - is based on the revolutionary developments which have been achieved in protein analysis during the last years. The number of finished genome projects is growing and in parallel there is a dramatically increasing need to identify the products of revealed genes. Acting on a micro level modern protein chemistry increases our understanding of biological events by elucidating the relevant structure-function relationships. The second edition of the successful title Microcharacterization of Proteins presents a current overview of modern protein analysis: From sample preparation to sequence analysis, mass spectrometry and bioinformatics it informs about the tools needed in protein research. This makes the book indispensable for everyone involved in proteomics!

Author : Roza Maria Kamp
Publisher : Springer Science & Business Media
Page : 311 pages
File Size : 47,60 MB
Release : 2012-12-06
Category : Science
ISBN : 3642592198

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"Protein Structure Analysis - Preparation and Characterization" is a compilation of practical approaches to the structural analysis of proteins and peptides. Here, about 20 authors describe and comment on techniques for sensitive protein purification and analysis. These methods are used worldwide in biochemical and biotechnical research currently being carried out in pharmaceu tical and biomedical laboratories or protein sequencing facilities. The chapters have been written by scientists with extensive ex perience in these fields, and the practical parts are well documen ted so that the reader should be able to easily reproduce the described techniques. The methods compiled in this book were demonstrated in student courses and in the EMBO Practical Course on "Microsequence Analysis of Proteins" held in Berlin September 10-15, 1995. The topics also derived from a FEBS Workshop, held in Halkidiki, Thessaloniki, Greece, in April, 1995. Most of the authors participated in these courses as lecturers and tutors and made these courses extremely lively and successful. Since polypeptides greatly vary depending on their specific structure and function, strategies for their structural analysis must for the most part be adapted to each individual protein. Therefore, advantages and limitations of the experimen tal approaches are discussed here critically, so that the reader becomes familiar with problems that might be encountered.

Author : Julian Whitelegge
Publisher : Elsevier
Page : 563 pages
File Size : 16,62 MB
Release : 2008-10-09
Category : Science
ISBN : 0080932037

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This book is designed to be a central text for young graduate students interested in mass spectrometry as it relates to the study of protein structure and function as well as proteomics. It is a definite must-have work for:- libraries at academic institutions with Master and Graduate programs in biochemistry, molecular biology, structural biology and proteomics- individual laboratories with interests covering these areas - libraries and individual laboratories in the pharmaceutical and biotechnology industries. *Serves as an essential reference to those working in the field*Incorporates the contributions of prominent experts *Features comprehensive coverage and a logical structure

Author : Kevin Downard
Publisher : John Wiley & Sons
Page : 153 pages
File Size : 29,93 MB
Release : 2007-08-24
Category : Science
ISBN : 047014632X

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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.

Author : Gwenael Pottiez
Publisher : Springer
Page : 77 pages
File Size : 33,40 MB
Release : 2015-02-05
Category : Science
ISBN : 3319130870

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The understanding of the events taking place in a cell, a biological fluid or in any biological system is the main goal of biology research. Many fields of research use different technology to assess those events. Mass spectrometry is one of those techniques and this undergoes constant evolution and adaptation to always enhance the accuracy of the information provided. Proteomics provides a large panel of data on protein identity and protein expression that were made possible by mass spectrometry. For several years now mass spectrometry has become central to performing proteomic research, however this powerful tool is under constant evolution to be more sensitive and more resolute. More importantly mass spectrometry became a field of research focusing on new applications. Indeed, the complexity in biological systems relies on the changes of expression of transcription of proteins but also on the post-translational modification of proteins, the structure of proteins and the interaction between proteins, amongst others. As of now, several investigations tried to improve the quantification of proteins by mass spectrometry, the determination of post-translational modifications, the protein-protein and protein-nucleic acids interaction or the proteins structures. This book is structured as follows: after a brief introduction of the usual and most popular applications for mass spectrometry in proteomics, the most recent research and developments in mass spectrometry-based methodologies will be explored.

Author : Brigitte Wittmann-Liebold
Publisher : Springer Science & Business Media
Page : 608 pages
File Size : 18,88 MB
Release : 2012-12-06
Category : Science
ISBN : 3642738346

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"Methods in Protein Sequence Analysis - 1988" - contains selected contributions on modern protein- analytical techniques as presented by speakers at the Seventh International Conference on "Methods in Protein Sequence Analysis", held from July 3rd to July 8th, 1988 in Berlin. The book contains information on new methodologies for sensitive amino acid analysis, N- and C-terminal sequence analysis, and protein and peptide purification. In addition recent mass spectrometric approaches are described, as an alter native technique to the common stepwise degradative sequence analysis of polypeptides by the Edman method. The book presents new possibilities in the design of sequencers and sophisticated equipment for the structural analysis of peptides and proteins. It describes practical approaches for the investigation of protein domains and protein complexes, and contains review chapters on the crystallization of cell organelles as well as on recent theoretical aspects of protein folding mechanisms. The nature of protein folding is not yet understood, but further advances in this area would greatly enhance our present knowledge of protein structure and function. Further, the book gives examples of the application of gene technology to protein characterization and to the design of new proteins. This enables new studies on the structure and function of proteins to be made, and opens up efficient approaches to the design of drugs.