Structural Characterization and Separation of Biomolecules by Matrix-assisted Laser Desorption Ionization Ion-mobility Mass Spectrometry PDF Download

Author: Ablatt Mahsut
Publisher:
ISBN:
Category : Biomolecules
Languages : en
Pages : 162

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Author: Whitney Beth Parson
Publisher:
ISBN:
Category : Electronic dissertations
Languages : en
Pages : 138

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Author: Bindesh Shrestha
Publisher: Elsevier
ISBN: 0128189991
Category : Science
Languages : en
Pages : 272

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Book Description
Imaging mass spectrometry (MS) techniques are often utilized without an understanding of their underlying principles, making it difficult for scientists to determine when and how they can exploit MS to visualize their biomolecules of interest. Introduction to Spatial Mapping of Biomolecules by Imaging Mass Spectrometry is an essential reference to help scientists determine the status and strategies of biomolecule analysis, describing its many applications for diverse classes of biomolecules. The book builds a foundation of imaging MS knowledge by introducing ionization sources, sample preparation, visualization guidelines, molecule identification, quantification, data analysis, etc. The second section contains chapters focused on case studies on analyzing a biomolecule class of molecules. Case studies include an introduction/background, and a summary of successful imaging MS studies with illustrative figures and future directions. Provides the introductory foundations of imaging mass spectrometry for those new to the technique Organized by topic to facilitate a quick deep dive, allowing researchers to immediately apply the imaging MS techniques to their work Includes case studies summarizing the imaging MS techniques developed for the class of molecules

Author: Anissa Wai-Sinn Wong
Publisher:
ISBN:
Category :
Languages : en
Pages : 256

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Author: Rainer Cramer
Publisher: Springer
ISBN: 3319048198
Category : Science
Languages : en
Pages : 287

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This book covers the state-of-the-art of modern MALDI (matrix-assisted laser desorption/ionization) and its applications. New applications and improvements in the MALDI field such as biotyping, clinical diagnosis, forensic imaging, and ESI-like ion production are covered in detail. Additional topics include MS imaging, biotyping/speciation and large-scale, high-speed MS sample profiling, new methods based on MALDI or MALDI-like sample preparations, and the advantages of ESI to MALDI MS analysis. This is an ideal book for graduate students and researchers in the field of bioanalytical sciences. This book also: • Showcases new techniques and applications in MALDI MS • Demonstrates how MALDI is preferable to ESI (electrospray ionization) • Illustrates the pros and cons associated with biomarker discovery studies in clinical proteomics and the various application areas, such as cancer proteomics

Author: Frederik Lermyte
Publisher: Royal Society of Chemistry
ISBN: 1839161108
Category : Science
Languages : en
Pages : 359

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Breaking down large biomolecules into fragments in a controlled manner is key to modern biomolecular mass spectrometry. This book is a high-level introduction, as well as a reference work for experienced users, to ECD, ETD, EDD, NETD, UVPD, SID, and other advanced fragmentation methods. It provides a comprehensive overview of their history, mechanisms, instrumentation, and key applications. With contributions from leading experts, this book will act as an authoritative guide to these methods. Aimed at postgraduate and professional researchers, mainly in academia, but also in industry, it can be used as supplementary reading for advanced students on mass spectrometry or analytical (bio)chemistry courses.

Author: Teresa Catherine Cain
Publisher:
ISBN:
Category :
Languages : en
Pages : 234

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Author: Jingshu Guo
Publisher:
ISBN:
Category : Electrospray ionization mass spectrometry
Languages : en
Pages : 405

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Book Description
Mass spectrometry (MS) has become one of the most robust, reliable and widely used analytical techniques in scientific research due to factors like its speed of analysis, ease of operation, high sensitivity, and applicability to a broad range of analytes. The development of the so-called "soft" ionization methods electrospray ionization (ESI) and matrix-assisted laser desorption/ionization (MALDI) played a pivotal role in the application of MS to biochemical and biophysical fields enabling comprehensive studies of biomolecules, macromolecules and their complexes. This dissertation presents method development and the application of MS-based strategies for complete sequence and structure determination of hemoglobin (Hb); investigation of the interaction between human Hb and Band 3; characterization of the interaction between Alanyl-tRNA synthetase with tRNA and various ligands; and characterization of various thiol-protected silver nanoclusters. First, the complete primary amino acid sequences of hemoglobin from the endangered species snow leopard (Uncia uncia), Amur tiger (Panthera tigris altaica), Cheetah (Acinonyx jubatus) and Francois' Langur (Trachypithecus francoisi) were determined using a combination of the bottom-up approach to proteomics in combination with single crystal X-ray diffraction. In this approach, MS was used to provide on average 70% coverage of the sequences, which was used in refinement of the diffraction data. The electron density maps from the diffraction data were used to determine the parts of the sequences not covered by MS as well as differentiate between isomeric residues. During the refinement of the X-ray diffraction data, a unique conformational state, the Bform, for naturally occurring ligated hemoglobin was discovered in two feline Hbs. Structural comparisons and possible biological relevance for the B-form will be presented. The binding of human hemoglobin to synthetic peptides corresponding to the Hb-binding sites of human erythrocyte Band 3 is also presented. The effects on binding of ligation and oxidation state of normal human HbA; human sickle HbS; Hb-binding site and peptide length; and Band 3 N-terminal acetylation were investigated. The optimization of MS instrumental parameters and solution conditions for stabilizing and protecting labile thiol-protected silver nanoclusters through ionization, mass analysis and detection is presented. The relatively much more stable and well characterized gold-glutathione cluster Au25(SG)18 was used as a model for instrumental optimization (SG, glutathione). The most crucial instrumental parameters to protecting the clusters were cone gas flow rate, trap/transfer collision energy, and source temperature. Using these optimized parameters and adjustment of solution conditions led to the formula assignment for Ag32(SG)19, the species isolated from band 6 of a polyacrylamide gel electrophoretic separation. Using a similar approach the formula assignment for Ag44L30-4 (L, p-mercaptobenzoic acid) was confirmed. Collision induced dissociation (CID) studies were used to demonstrate that Ag43L28-3, another abundant species in the mass spectra was in fact a fragment of the intact cluster from the facile loss of AgL2-. CID and ion mobility mass spectrometry (IMMS) of Au25(SG)18, Ag32(SG)19, and Ag44L30-4 were used to gain insight into the surface structure and stability of the fragile silver clusters. Finally, the 3'-tRNA binding site on E. coli Alanyl-tRNA synthetase was identified by first crosslinking the 3'-periodate-oxidized tRNAala to the enzyme followed by the bottom-up MS sequencing. Modified lysine residues identified were 74, 526 585, 637, 739 and 648. Lys 74 was in the aminoacylation domain while 526 585, 637, 739 and 648 were in the editing domain. These results highlight an alteration of the 3'-terminal of tRNAala interaction with the enzyme. To study the stability ARS with various ligands, non-hydrolysable adenylate analogs, ASAd and GSAd, were used. Data shows that complete binding of ASAd and GSAd was achieved and that binding occurred in a 1:1 stoichiometry. Binding of ASAd, the analog of the cognate ligand, stabilizes the enzyme against changes in solution pH relative to the apo-enzyme and the enzyme with GSAd bound.

Author: Steven Travis Fannin
Publisher:
ISBN:
Category :
Languages : en
Pages : 312

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Author: W. Ens
Publisher: Springer Science & Business Media
ISBN: 940159046X
Category : Science
Languages : en
Pages : 350

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Book Description
A NATO Advanced Research Workshop entitled New Methods for the Study of Molecular Aggregates was held at Tbe Lodge at Kananaskis Village, Alberta, Canada from 16 -20 June 1996. In fact the meeting was entirely concerned with the problem of analyzing biomolecular complexes, so the title of these proceedings has been altered to give a more precise description of the content. Tbe workshop was hosted by the time-of-flight group of the Department of Physics at the University of Manitoba, and was attended by 64 participants from around the world. '!\venty-one invited talks were given and 27 papers were presented as posters. Of the 48 contributions, 22 papers (12 orals, 10 posters) are included in these proceedings. Tbe subject of the conference was the investigation of noncovalent biomolecular complexes, with particular focus on the application of mass spectrometry to their characterization. '!\vo new ionization techniques introduced in the late 1980s, electrospray ionization (ES I) and matrix-assisted laser desorptionlionization (MALDI), resulted in a breakthrough in mass spectrometry, enabling its use in molecular weight and primary structure determination of biopolymers larger than 100 kDa. Recently it has been discovered that ESI mass spectrometry mayaiso be used to characterize complexes containing noncovalent interactions, thus opening new perspectives for supramolecular chemistry. ESI mass spectrometry has the advantage that the sampie is introduced from a homogenous solution which can be maintained at near physiological conditions of pR, concentration, and temperature.