Laser Photodissociation and Spectroscopy of Mass-separated Biomolecular Ions

Laser Photodissociation and Spectroscopy of Mass-Separated Biomolecular Ions (Paperback)
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The implementation of laser- based photodissociation techniques in MS requires basic knowledge of tunable light sources and ion trapping devices. This book introduces the reader to key concepts and approaches in molecular spectroscopy, and the light sources and ion traps employed in such experiments. The power of the methods is demonstrated by spectroscopic interrogation of a range of important biomolecular systems, including peptides , proteins , and saccharides , with laser light in the ultraviolet-visible, and infrared range.

Infrared multiphoton dissociation

It provides the solid background of key concepts and technologies for the measurements, discusses state-of-the-art experiments, and provides an outlook on future developments and applications. JavaScript is currently disabled, this site works much better if you enable JavaScript in your browser.

Introduction

Hathout et al. Physica Scripta. Partridge, and S. Advanced Book Search Browse by Subject. It reports the successful construction ofa novel decay spectroscopy apparatus that can operate at pressures below

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Edited by two renowned experts for UV-vis and IR laser based photodissociation and spectroscopy in MS of biomolecules Introduces methods combining mass spectrometry MS and spectroscopy - a particularly powerful combination for enhanced structural information on biomolecules Explains the basics, from fundamentals about spectroscopy over tunable light sources to ion trapping devices Demonstrates the power of spectroscopic interrogation of biomolecules, from peptides, over proteins, to saccharides; in the present state-of-the-art, and in an outlook on future developments see more benefits.

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ISBN 10: 3319012517

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Laser Photodissociation and Spectroscopy of Mass-separated Biomolecular Ions

Photodissociation has been extensively explored in the last decades for the analysis of peptides and proteins by mass spectrometry MS. In the photodissociation process, ions interact with photons generating an increment on internal energy that leads to their fragmentation. The specific characteristics of photodissociation techniques have led to improvements in different applications of MS.

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Among them, the cleavage of molecular bonds in a selective manner, based on the incorporation of chromophore molecules. Moreover, the ability to generate an almost complete array of fragment ions is the main reason for the increment in the utilization of ultraviolet photodissociation UVPD. This technique has been applied to the most challenging proteomics studies, such as the characterization of posttranslational modifications and protein sequence variations, de novo sequencing, and the analysis of intact proteins.

This article is focused on the most recent and relevant developments of infrared photodissociation and UVPD techniques and their application to the study of peptides and proteins.

FRAGMENTATIUON PATTERN OF ORGANIC MOLECULES UNDER ELECTRON IONIZATION MASS SPECTROMETRY II

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