Identification of carbonylation sites in apomyoglobin after exposure to 4-hydroxy-2-nonenal by solid-phase enrichment and liquid chromatography-electrospray ionization tandem mass spectrometry.: This research identifies specific carbonylation sites in apomyoglobin following exposure to 4-hydroxy-2-nonenal, using advanced mass spectrometry techniques for precise localization of oxidative modifications. (Rauniyar et al., 2010).
Analysis of heterogeneous fluorescence decays in proteins. Using fluorescence lifetime of 8-anilino-1-naphthalenesulfonate to probe apomyoglobin unfolding at equilibrium.: This study uses fluorescence lifetime measurements to analyze the unfolding processes of apomyoglobin, providing insights into protein stability and folding dynamics. (Wang et al., 2006).
