Download e-book for kindle: Biological Mass Spectrometry by A. L. Burlingame (Eds.)

By A. L. Burlingame (Eds.)

ISBN-10: 0121828077

ISBN-13: 9780121828073

This quantity describes and integrates the ideas and basics of greater than a decade of innovative advances in either chromatographic and mass spectrometric applied sciences that experience enabled the direct research of biomacromolecules in line with se and feature supplied the analytical strength base to herald the hot fields of proteomics and structures biology.

It additionally covers new biophysical functions akin to H/D alternate for learn of conformations, protein-protein and protein-metal and ligand interactions. ultimately it describes atto-to-zepto-mole quantitation of 14C and 3H through accelerator mass spectrometry.

*Part 1 of two volumes approximately Mass Spectrometry
*Authoritative and entire remedy of protein mass spectrometry in human mobilephone biology
*Presents basics, innovations, instrumentation and bioinformatics
*Provides an outline of proteomics, protein-protein and protein-ligand binding, and biophysical stories

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Extra resources for Biological Mass Spectrometry

Example text

72, 652–657. Levsen, K. (1978). ’’ Verlag Chemie, Weinheim. , Anderson, G. , Lipton, M. , Conrads, T. , and Smith, R. D. (2001). High‐throughput peptide identification from protein digests using data‐dependent multiplexed tandem FTICR mass spectrometry coupled with capillary liquid chromatography. Anal. Chem. 73, 3312. Loo, J. A. (1997). Studying noncovalent protein complexes by electrospray ionization mass spectrometry. Mass Spectrom. Rev. 16, 1–23. Mamyrin, B. , and Shmikk, D. V. (1979). The linear mass reflectron.

A Qq‐time‐of‐flight tandem mass spectrometer. , 1997). For MS/MS operation, the mass range is limited by the maximum m/z selectable by the quadrupole, typically 3000, but because most CID experiments for biopolymer characterization are carried out on smaller fragments, such as peptides from a digested protein, this is generally adequate. As described earlier, to improve the duty cycle and, therefore, the sensitivity of the QqTOF for low mass ions by up to 20 times, one manufacturer has introduced a degree of mass‐dependent trapping immediately before the accelerator.

2000), although there have been few demonstrated examples of this approach. For protein analysis, the performance specifications of most high‐performance tandem mass spectrometers such as the QqTOF are relevant only to the analysis of fragments (peptides) but not to intact proteins. By contrast, the FT‐ICR is capable of isotopic resolution of intact proteins. Ion activation can be induced by infrared laser radiation, resulting in multiphoton dissociation, or by pulsed admission of CID gases. However, it is difficult to introduce sufficient energy through collisions of large ions with light gases to achieve significant fragmentation and only the lowest energy pathways are populated, so conventional CID on large proteins is relatively uninformative.

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Biological Mass Spectrometry by A. L. Burlingame (Eds.)

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