Exploring the feasibility and usability of the experience sampling method to examine the daily lives of patients with acquired brain injury

The experience samplingmethod (ESM) is a structured diarymethod with high ecological validity, in that it accurately captures the everyday context of individuals through repeated measurements in naturalistic environments. Our main objective was to investigate the feasibility of using ESM in individuals with acquired brain injury (ABI). A second goal was to explore the usability of ESM data on a clinical level, by illustrating the interactions between person, environment, and affect. The PsyMate device provided ABI patients (N = 17) with ten signals (beeps) per day during six consecutive days. Each beep was followed by a digital questionnaire assessing mood, location, activities, social context, and physical well-being. Results demonstrated high feasibility with a 71% response rate and a 99% completion rate of the questionnaires. There were no dropouts and the method was experienced as user-friendly. Time-lagged multilevel analysis showed that higher levels of physical activity and fatigue predicted higher levels of negative affect at the same point in time, but not at later time points. This study illustrates the potential of ESM to identify complex person–environment dynamics after ABI, while generating understandable and easy to use graphical feedback

Is the heme pocket region modulated by disulfide-bridge formation in fish and amphibian neuroglobins as in humans?

Abstract: Neuroglobin, a globin characterized by a bis-histidine ligation of the heme iron, has been identified in mammalian and non-mammalian vertebrates, including fish, amphibians and reptiles. In human neuroglobin, the presence of an internal disulfide bond in the CD loop (CD7D5) is found to modulate the ligand binding through a change in the heme pocket structure. Although the neuroglobin sequences mostly display conserved Cys at positions CD7, D5 and G18/19, a number of exceptions are known. In this study, neuroglobins from amphibian (Xenopus tropicalis) and fish (Chaenocephalus aceratus, Dissostichus mawsoni and Danio rerio) are investigated using electron paramagnetic resonance and optical absorption spectroscopy. All these neuroglobins differ from human neuroglobin in their Cys-positions. It is demonstrated that if disulfide bonds are formed in fish and amphibian neuroglobins, the reduction of these bonds does not result in alteration of the heme pocket in these globins. Furthermore, it is shown that mutagenesis of the Cys residues of X. tropicalis neuroglobin influences the protein structure. The amphibian neuroglobin is also found to be more resistant to H2O2-induced denaturation than the other neuroglobins under study, although all show an overall large stability in high concentrations of this oxidant. This article is part of a Special Issue entitled: Oxygen Binding and Sensing Proteins