ArticleMethods in molecular biology (Clifton, N.J.)2026
Applying Surface Plasmon Resonance to the Study of Striated Muscle Protein Interactions.
Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Surface Plasmon Resonance (SPR) is a powerful tool for measuring binding interactions, especially in biological systems where many interactions have binding affinities in the nanomolar to micromolar range. SPR has been used to investigate binding interactions in a wide range of systems but has largely not been used to explore striated muscle protein interactions. This chapter outlines the method that our labs have used to measure binding interactions involving striated muscle proteins. The first method focuses on binding of a calcium-binding protein to the titin protein in a traditional SPR binding experiment. The second method focuses on the multi-site binding of truncated fragments of the regulatory protein troponin T (TnT1) to the tropomyosin-filamentous actin (Tpm/F-actin) thin filament complex, which involves multiple interaction sites. These two approaches highlight the utility of using SPR to understand muscle protein interactions.
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