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The study investigates the positioning of transmembrane α-helices in the GltPh glutamate transporter homolog, revealing that these helices can reposition during membrane protein folding, contrary to traditional models. The findings indicate that the optimal placement of helices does not always align with their known three-dimensional structures, suggesting a need to revise existing models of membrane protein folding. This research highlights the complexities of membrane protein structure prediction and the

Author

jose miguel

Language

EN