6 research outputs found
Conscripts psychological testing results' relationship with mental and physical health
Psichologijos katedraVytauto Didžiojo universiteta
ProteināLigand Binding Volume Determined from a Single 2D NMR Spectrum with Increasing Pressure
[Image: see text] Proteins undergo changes in their partial volumes in numerous biological processes such as enzymatic catalysis, unfoldingārefolding, and ligand binding. The change in the protein volume upon ligand bindingāa parameter termed the proteināligand binding volumeācan be extensively studied by high-pressure NMR spectroscopy. In this study, we developed a method to determine the proteināligand binding volume from a single two-dimensional (2D) (1)Hā(15)N heteronuclear single quantum coherence (HSQC) spectrum at different pressures, if the exchange between ligand-free and ligand-bound states of a protein is slow in the NMR time-scale. This approach required a significantly lower amount of protein and NMR time to determine the proteināligand binding volume of two carbonic anhydrase isozymes upon binding their ligands. The proposed method can be used in other proteināligand systems and expand the knowledge about protein volume changes upon small-molecule binding
S100A9 Alters the Pathway of Alpha-Synuclein Amyloid Aggregation
The formation of amyloid fibril plaques in the brain creates inflammation and neuron death. This process is observed in neurodegenerative disorders, such as Alzheimerās and Parkinsonās diseases. Alpha-synuclein is the main protein found in neuronal inclusions of patients who have suffered from Parkinsonās disease. S100A9 is a calcium-binding, pro-inflammation protein, which is also found in such amyloid plaques. To understand the influence of S100A9 on the aggregation of Ī±-synuclein, we analyzed their co-aggregation kinetics and the resulting amyloid fibril structure by Fourier-transform infrared spectroscopy and atomic force microscopy. We found that the presence of S100A9 alters the aggregation kinetics of Ī±-synuclein and stabilizes the formation of a particular amyloid fibril structure. We also show that the solutionās ionic strength influences the interplay between S100A9 and Ī±-synuclein, stabilizing a different structure of Ī±-synuclein fibrils
Interactions between S100A9 and Alpha-Synuclein: Insight from NMR Spectroscopy
S100A9 is a pro-inflammatory protein that co-aggregates with other proteins in amyloid fibril plaques. S100A9 can influence the aggregation kinetics and amyloid fibril structure of alpha-synuclein (α-syn), which is involved in Parkinson’s disease. Currently, there are limited data regarding their cross-interaction and how it influences the aggregation process. In this work, we analyzed this interaction using solution 19F and 2D 15N–1H HSQC NMR spectroscopy and studied the aggregation properties of these two proteins. Here, we show that α-syn interacts with S100A9 at specific regions, which are also essential in the first step of aggregation. We also demonstrate that the 4-fluorophenylalanine label in alpha-synuclein is a sensitive probe to study interaction and aggregation using 19F NMR spectroscopy