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Function: require_once
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Function: _error_handler
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Function: _error_handler
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Function: insertAPISummary
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Filename: helpers/my_audit_helper.php
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Function: formatAIDetailSummary
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This work is focused at understanding the interaction of HS with Myoglobin (Mb), in particular the Sulfmyoglobin (SMb) product, whose physiological role is controversial and not well understood. The scattering curves, Guinier, Kratky, Porod and P(r) plots were analyzed for oxy-Mb and oxy-Hemoglobin I (oxyHbI) in the absence and presence of HS, using Small and Wide Angle X-ray Scattering (SAXS/WAXS) technique. Three dimensional models were also generated from the SAXS/WAXS data. The results show that SMb formation, produced by oxyMb and HS interaction, induces a change in the protein conformation where its envelope has a very small cleft and the protein is more flexible, less rigid and compact. Based on the direct relationship between Mb's structural conformation and its functionality, we suggest that the conformational change observed upon SMb formation plays a contribution to the protein decrease in O affinity and, therefore, on its functionality.
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http://dx.doi.org/10.1016/j.bbrep.2016.07.002 | DOI Listing |
FEMS Microbiol Lett
December 2024
Laboratory of Biotechnology, Chulabhorn Research Institute, Lak Si, Bangkok 10210, Thailand.
Stenotrophomonas maltophilia is an emerging global opportunistic pathogen that causes nosocomial infections. We demonstrated that the superoxide stress-sensing transcriptional regulator SoxR directly modulated the expression of an operon encompassing sodA1 (encoding manganese-containing superoxide dismutase) and fre (encoding putative flavin reductase) by directly binding to the operator site, which was located between the - 35 and -10 motifs of the sodA1 promoter. It is known that upon exposure to the superoxide generators/redox-cycling drugs, the SoxR, which is bound to the operator site, became oxidized.
View Article and Find Full Text PDFNeurobiol Dis
December 2024
Department of Neurology, Kanazawa University Graduate School of Medical Sciences, 13-1, Kanazawa 920-8640, Japan. Electronic address:
The accumulation of amyloid β-proteins (Aβ) in the extracellular space, forming insoluble plaques, is a primary pathological process underlying Alzheimer's disease (AD). Among the various Aβ species that appear during Aβ aggregation, Aβ oligomers are considered the most neurotoxic form. However, the precise mechanisms of their molecular functions within the Aβ aggregation cascade have not been clarified so far.
View Article and Find Full Text PDFJ Biomol Struct Dyn
December 2024
Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India.
Nucleocapsid protein (N) of SARS-CoV-2 is a multivalent protein, which is responsible for viral replication, assembly, packaging and modulates host immune response. In this study, we report conformational measurements of N protein at different pH by observing transition in secondary and tertiary structural contents by biophysical and computational approaches. Spectroscopic measurements revealed that N protein loses its secondary and tertiary structure at extreme acidic pH while maintaining its native conformation at mild acidic and alkaline pH.
View Article and Find Full Text PDFACS Appl Mater Interfaces
December 2024
Group of Characterization of Materials, Departament de Física, Universitat Politècnica de Catalunya, Campus Diagonal-Besòs, Av. Eduard Maristany 10-14, Barcelona 08019, Spain.
Hybrid organic-inorganic perovskites (HOIP) have emerged in recent years as highly promising semiconducting materials for a wide range of optoelectronic and energy applications. Nevertheless, the rotational dynamics of the organic components and many-molecule interdependencies, which may strongly impact the functional properties of HOIP, are not yet fully understood. In this study, we quantitatively analyze the orientational disorder and molecular correlations in archetypal perovskite CHNHPbI (MAPI) by performing comprehensive molecular dynamics simulations and entropy calculations.
View Article and Find Full Text PDFInt J Biol Macromol
December 2024
School of Health Science and Engineering, Shanghai Engineering Research Center of Food Rapid Detection, University of Shanghai for Science and Technology, Shanghai 200093, China. Electronic address:
Aptamer conformations are susceptible to environmental conditions, which makes it difficult to achieve stable targets detection in complex environments with aptasensors. Imprinting strategy was proposed to immobilize the specific conformation of aptamers, aiming to enhance their recognition anti-interference. However, it is mechanistically unclear how the imprinted polymers affect aptamers' recognition, which limits application of the strategy.
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