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In an era of interdisciplinary scientific research, new methodologies are necessary to simultaneously advance several fields of study. One such case involves the measurement of electron spin effects on biological systems. While magnetic effects are well known in biology, recent years have shown a surge in published evidence isolating the dependence on spin, rather than magnetic field, in biological contexts.

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Many proteins form paralogous multimers-molecular complexes in which evolutionarily related proteins are arranged into specific quaternary structures. Little is known about the mechanisms by which they acquired their stoichiometry (the number of total subunits in the complex) and heterospecificity (the preference of subunits for their paralogs rather than other copies of the same protein). Here, we use ancestral protein reconstruction and biochemical experiments to study historical increases in stoichiometry and specificity during the evolution of vertebrate hemoglobin (Hb), an αβ heterotetramer that evolved from a homodimeric ancestor after a gene duplication.

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Structural insights into glucose-6-phosphate recognition and hydrolysis by human G6PC1.

Proc Natl Acad Sci U S A

January 2025

Beijing National Laboratory for Condensed Matter Physics, Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, China.

The glucose-6-phosphatase (G6Pase) is an integral membrane protein that catalyzes the hydrolysis of glucose-6-phosphate (G6P) in the endoplasmic reticulum lumen and plays a vital role in glucose homeostasis. Dysregulation or genetic mutations of G6Pase are associated with diabetes and glycogen storage disease 1a (GSD-1a). Studies have characterized the biophysical and biochemical properties of G6Pase; however, the structure and substrate recognition mechanism of G6Pase remain unclear.

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A series of significantly bulky mono- and di-substituted cyclic alkyl-amino carbene (cAAC)- functionalized cyclopentadiene ring (Cp) compounds were synthesized. The functionalization of the Cp ring with cAAC ligands makes them significantly bulkier, while retaining their ligation properties. These compounds display interesting fluorescence properties.

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Molecular and Immunological Characterization of Troponin C: An Allergen from .

J Agric Food Chem

January 2025

College of Ocean Food and Biological Engineering, Xiamen Key Laboratory of Marine Functional Food, Fujian Provincial Engineering Technology Research Center of Marine Functional Food, National & Local Joint Engineering Research Center of Processing Technology for Aquatic Products, Jimei University, Xiamen, Fujian 361021, China.

, a crustacean of substantial importance, is a frequent trigger of food allergies. This study examined the molecular and immunological properties of troponin C from (Scy p TnC) as an allergen. The findings indicated that thermal stability of Scy p TnC comprised 150 amino acids and facilitated the induction of CD63/CD203c in basophils from crab allergy patients.

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