Phenotyping of human muscle based on its profile of myosin heavy chain isoforms is commonly used to help understand changes in muscle function. However, in many instances, measureable changes in force output or contractility occur in the absence of any change in myosin heavy chain profile. Therefore, more sophisticated analysis is required. Proteomic techniques including 2-dimensional gel electrophoresis, highperformance liquid chromatography and peptide mass spectrometry can be used to investigate changes in the abundance of hundreds of proteins simultaneously. To date, such techniques have not been used to specifically characterise the human myofibrillar proteome, or study how the myofibrillar proteome relates to muscle outputs such as peak isometric force or the velocity of contraction. This thesis presents a series of studies that develop proteomic techniques for the analysis of myofibrillar proteins as well as optimisation of techniques for measuring the range of muscle output fro.....

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