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Editorial for Special Issue: Approaches to Top-Down Proteomics: In Honour of Prof. Patrick H. O’Farrell
Erratum published on 15 July 2019, see Proteomes 2019, 7(3), 28.
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Characterization of Contractile Proteins from Skeletal Muscle Using Gel-Based Top-Down Proteomics

1
Department of Biology, Maynooth University, Maynooth, W23F2H6 Co. Kildare, Ireland
2
MU Human Health Research Institute, Maynooth University, Maynooth, W23F2H6 Co. Kildare, Ireland
3
Institute of Physiology II, University of Bonn, D-53115 Bonn, Germany
*
Author to whom correspondence should be addressed.
Proteomes 2019, 7(2), 25; https://doi.org/10.3390/proteomes7020025
Received: 29 May 2019 / Revised: 14 June 2019 / Accepted: 17 June 2019 / Published: 20 June 2019
(This article belongs to the Special Issue Top-down Proteomics: In Memory of Dr. Alfred Yergey)
The mass spectrometric analysis of skeletal muscle proteins has used both peptide-centric and protein-focused approaches. The term ‘top-down proteomics’ is often used in relation to studying purified proteoforms and their post-translational modifications. Two-dimensional gel electrophoresis, in combination with peptide generation for the identification and characterization of intact proteoforms being present in two-dimensional spots, plays a critical role in specific applications of top-down proteomics. A decisive bioanalytical advantage of gel-based and top-down approaches is the initial bioanalytical focus on intact proteins, which usually enables the swift identification and detailed characterisation of specific proteoforms. In this review, we describe the usage of two-dimensional gel electrophoretic top-down proteomics and related approaches for the systematic analysis of key components of the contractile apparatus, with a special focus on myosin heavy and light chains and their associated regulatory proteins. The detailed biochemical analysis of proteins belonging to the thick and thin skeletal muscle filaments has decisively improved our biochemical understanding of structure-function relationships within the contractile apparatus. Gel-based and top-down proteomics has clearly established a variety of slow and fast isoforms of myosin, troponin and tropomyosin as excellent markers of fibre type specification and dynamic muscle transition processes. View Full-Text
Keywords: actin; mass spectrometry; muscle proteomics; myosin; top-down proteomics; tropomyosin; troponin; two-dimensional gel electrophoresis; skeletal muscle actin; mass spectrometry; muscle proteomics; myosin; top-down proteomics; tropomyosin; troponin; two-dimensional gel electrophoresis; skeletal muscle
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Dowling, P.; Zweyer, M.; Swandulla, D.; Ohlendieck, K. Characterization of Contractile Proteins from Skeletal Muscle Using Gel-Based Top-Down Proteomics. Proteomes 2019, 7, 25.

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