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Wednesday, July 22, 2020 | History

2 edition of Strategies for peptide and protein analysis by fast atom bombardment mass spectrometry. found in the catalog.

Strategies for peptide and protein analysis by fast atom bombardment mass spectrometry.

Malcolm Ronald Clench

Strategies for peptide and protein analysis by fast atom bombardment mass spectrometry.

by Malcolm Ronald Clench

  • 261 Want to read
  • 16 Currently reading

Published .
Written in English


Edition Notes

ContributionsManchester Polytechnic. Department of Biological Sciences., Manchester Polytechnic. Department of Chemistry.
ID Numbers
Open LibraryOL13905927M

Chait, B.T. () The use of Cf plasma desorption mass spectrometry for the analysis of synthetic peptides and proteins, in The Analysis of Peptides and Proteins by Mass Spectrometry (McNeal, J., ed.), John Wiley, New York, p. Google Scholar.   These two ionization methods will be detailed in this page along with methods used prior to these discoveries such as electron bombardment (EI) and fast atom bombardment (FAB). A few applications of Mass spectrometry for membrane protein analysis will also be covered.

  Fast Atom Bombardment (FAB) However, for many of these ionization methods, applications in the peptide or protein space simply aren't reasonable. Methods like APCI, EI and FAB are often much too aggressive for analyzing peptides as they often result in fragmentation of the compounds of interest. ISBN: X OCLC Number: Description: XIV, Seiten: Diagramme ; 24 cm: Contents: De Novo Peptide Sequencing by Nanoelectrospray Tandem Mass Spectrometry Using Triple Quadrupole and Quadrupole/Time-of-Flight Instruments Andrej Shevchenko, Igor Chernushevich, Matthias Wilm, and Matthias Mann Direct Analysis of Proteins in Mixtures: Application to Protein.

  Henzel WJ, Bourell JH, Stults JT. Analysis of protein digests by capillary high-performance liquid chromatography and on-line fast atom bombardment mass spectrometry. Anal Biochem. Jun; (2)– Henzel WJ, Rodriguez H, Watanabe C. Computer analysis of automated Edman degradation and amino acid analysis data. J Chromatogr. A multiple mass spectrometric strategy using fast-atom bombardment (FAB) and matrix-assisted laser desorption/ionization (MALDI) has been used to confirm the sequence and to locate the disulfide linkages of recombinant maxadilan (r-maxadilan) (average molecular mass Da), a potent vasodilatory peptide from Lutzomyia longipalpis.


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Strategies for peptide and protein analysis by fast atom bombardment mass spectrometry by Malcolm Ronald Clench Download PDF EPUB FB2

The introduction of fast atom bombardment (FAB) in revolutionized organic mass spectrometry in that it provided an easy and convenient method for ionizing thermally unstable molecules with masses up to ∼10 kDa. It developed from surface ionization methods in which beams of fast atoms or ions are used to sputter ions from solid surfaces.

The main technical challenge has been the coupling of liquid chromatography (LC) systems with mass spectrometers.

Soft ionization techniques that have contributed to HPLC/MS for peptide and protein study include fast atom bombardment (FAB), matrix‐assisted laser desorption/ionization (MALDI), and electrospray ionization (ESI).Author: Tun‐Li Shen.

3 Fast-atom bombardment (FAB) Historically, FAB-MS has played an important role in the development of MS-based lipid analyses. Many fragmentational patterns of different polar lipid classes have been elucidated by either through-source decay fragmentation [37, ] or by FAB tandem mass spectrometry over more than 25 years [,].

Fast Atom Bombardment Mass Spectrometry. Fast Atom Bombardment Mass Spectrometry (FAB-MS) is is a very powerful technique utilising a stream of fast atoms such as argon to achieve ionisation in the mass spectrometer.

This is a "soft" ionisation technique. Van Bremen, R B. and Le, J C. () Enhanced sensitivity of peptide analysis by fast atom bombardment mass spectrometry using nitrocellulose as a substrate. Rapid. Commun Mass. Spectrom 3, 20– CrossRef Google ScholarCited by: 1.

In Mass Spectrometry of Proteins and Peptides, John R. Chapman recreates the success of his earlier acclaimed book (Protein and Peptide Analysis by Mass Spectrometry, ) with a major new collection of cutting-edge methods in this area. The purpose of the preface is to explain the book's objectives and how to use it; give warnings, disclaimers, and the like.* The main objective of Protein and Peptide Analysis by Mass Spec­ trometry is quite straightforward—to present authoritative, up-to-date, and practical accounts of the use of mass spectrometry in the analysis of pep­ tides and proteins.

Peptide mass fingerprinting (PMF) grew from a need for a faster, more efficient method to identify frequently observed proteins in electrophoresis gels. We describe the genesis of the idea inand show the first demonstration with fast atom bombardment mass spectrometry.

Despite its promise, the method was seldom used untilwith the coming of significantly more sensitive commercial. 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.

Peptide mass fingerprinting (PMF) grew from a need for a faster, more efficient method to identify frequently observed proteins in electrophoresis gels.

We describe the genesis of the idea inand show the first demonstration with fast atom bombardment mass spectrometry. The strategy implied the use of fast atom bombardment (FAB) or plasma-desorption MS to determine the masses of the proteolytic fragments produced by a specific enzyme or chemical. The experimental data was then compared with the masses predicted from all three reading frames of the gene sequences in order to verify the protein sequence or show.

The fastest method for protein identifi cation is the peptide mass fi ngerprinting (PMF) approach. and fast atom bombardment widely used protease in protein mass spectrometry analysis. The choice of approach for analyzing glycoprotein samples using fast-atom bombardment-mass spectrometry (FAB-MS) is dependent on the information required (see Scheme only the carbohydrate portion of the molecule is of interest, then N-linked glycans may be released directly from the intact glycoprotein using peptide-N 4-(N-acetyl-β-glucosaminyl) asparagine amidase F (PNGase.

Gonzalez J, Takao T, Hori H, et al. A method for determination of N-glycosylation sites in glycoproteins by collision-induced dissociation analysis in fast atom bombardment mass spectrometry: identification of the positions of carbohydrate-linked asparagine in recombinant alpha-amylase by treatment with peptide-N-glycosidase F in 18O-labeled water.

Application of mass spectrometric data for protein identification was tested using the fast atom bombardment (FAB) mass spectrum of trypsin digested lysozyme. The lysozyme was successfully identified by correlating the measured peptide mass with the already existing peptide mass of lysozyme by using a computer program called FRAGFIT.

Throck Watson's 74 research works with 3, citations and 2, reads, including: Introduction to Mass Spectrometry: Instrumentation, Applications and Strategies for Data Interpretation. Large-scale protein identifications from highly complex protein mixtures have recently been achieved using multidimensional liquid chromatography coupled with tandem mass spectrometry (LC/LC−MS/MS) and subsequent database searching with algorithms such as SEQUEST.

Here, we describe a probability-based evaluation of false positive rates associated with peptide identifications. Sequence Analysis of Protein C-Terminal Proteolytic Fragments, Protein Isolated from 2D-gels, and Murine Calbindin: New Methodology Location of Disulfide Bonds in Proteins by Partial Acid Hydrolysis and Mass Spectrometry Evaluation of Methods for the Analysis of Disulfide Containing Peptides by Fast Atom Bombardment Mass.

De Novo peptide sequencing by nanoelecrospray tandem mass spectrometry using triple quadrupole and quadrupole/time-of-flight instruments --Direct analysis of proteins in mixtures: application to protein complexes --Characterizaton of a mutant recombinant S protein using electrospray ionization mass spectrometry --Searching sequence databases.

Several complementary peptide maps are constructed using fast atom bombardment mass spectrometry (FAB-MS) analysis of different proteolytic digests of the unknown protein and the mass values are related to those expected on the basis of the sequence of the reference protein.

The mass signals exhibiting unusual mass values identify those regions. Fast atom bombardment /mass spectrometry (FAB/MS) was recognized early as being a useful method for establishing the structure of PtdIns. This is due to the unique chemical behavior of this compound having a highly lipophilic region, which enables the molecule to orient on the surface of FAB-matrices, as well as polar functionalities, which readily accept negative charge sites in the gas phase.Fast atom bombardment mass spectrometry has been used to confirm and correct regions from the amino acid sequences of three large proteins, glutaminyl- and glycyl-tRNA synthetase from Escherichia."Protein and Peptide Analysis by Mass Spectrometry" is a very good handbook for beginners, as well as experienced people.

It is written by some of the best world specialists in the field. Volume 61 of the famous "Methods in Molecular Biology" series, it is built on the usual format: Introduction, Materials, Methods and s: 1.