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Neuroproteomics: Methods and Protocols

Neuroproteomics: Methods and Protocols

Paperback

Series: Methods in Molecular Biology, Book 566

Medical ReferenceAnatomy & Physiology

ISBN10: 1617797545
ISBN13: 9781617797545
Publisher: Springer Nature
Published: Jul 12 2012
Pages: 321
Weight: 1.67
Height: 0.70 Width: 8.25 Depth: 11.00
Language: English
Neuroproteomics: Methods and Protocols presents experimental details for applying proteomics to the study of the central nervous system (CNS) and its dysfunction through trauma and disease. The target audience includes clinical or basic scientists who look to apply proteomics to the neurosciences. Often researchers hear of proteomics without an adequate explanation of the methodology and inherent limitations. This volume conveys where proteomic methodology is in its application to CNS research and what results can be expected. We also address clinical translation of neuroproteomics, specifically in the area of biomarker research. The inception of neuroproteomics capitalized on rapid progress in large-molecule mass spectrometry over the last decade. Two seminal advances have spurred research - development of reliable polypeptide ionization processes and bioinformatics to rapidly process tandem mass spectra for peptide identification and quantification. What has followed is the exponential application of mass spectrometry to proteome characteri- tion across biological and biomedical disciplines. Arguably, the most elaborate proteomic implementation is in studying the CNS, the most enigmatic and complex animal system. Neuroscience is characterized by grandiose questions - what is consciousness, how does thought or memory work. Neuroproteomics researchers, however, have pri- rily involved themselves dysfunction, based on a pressing need (and invariably funding), in answering questions on CNS dysfunction, based on a pressing need (and invariably funding), and because such questions hold more accessible answers. Dysfunction is readily contrasted against normal function and presumably produces a lasting differential protein signature.

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