Jan S Pedersen

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In this study, the experimental techniques scanning electron microscopy (SEM) including energy-dispersive X-ray analysis, atomic force microscopy (AFM) and scanning small angle X-ray scattering (SAXS) have been exploited to characterize the organization of large molecules and nanocrystallites in and around the neurocentral growth plate (NGP) of a pig(More)
Bovine α-lactalbumin (aLA) and oleate (OA) form a complex that has been intensively studied for its tumoricidal activity. Small-angle X-ray scattering (SAXS) has revealed a lipid core surrounded by partially unfolded protein. We call this type of complex a liprotide. Little is known of the molecular interactions between OA and aLA and no technique has so(More)
Proteins and lipids can form complexes called liprotides, in which the partially denatured protein forms a shell encasing a lipid core. This effectively stabilizes a lipid micelle in an aqueous solvent and suggests that liprotides may provide a suitable vessel for membrane proteins. Accordingly we have investigated if liprotides consisting of α-lactalbumin(More)
Arlaud et al. (1) raised concerns regarding our smallangle X-ray scattering (SAXS) and EM models of the unbound C1r2s2 tetramer (2). They reference studies supporting an interaction of two C1rs dimers via C1r CCP1–serine protease (SP) interactions. In response, we conducted refinements against our SAXS data by imposing distance restraints derived from C1r(More)
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