A new publication in Acta Materia Medica discusses studying conformational changes induced by protein mutations, essential for understanding mutation-related processes. The paper introduces a method using adversarial attacks on the AlphaFold2 model to generate mutated proteins, reducing experimental time and cost. Results show that altering three residues led to significant differences in AF2 predictions. The method was applied to the SPNS2 transmembrane lipid transporter to identify crucial residues and suggest alternative conformations, aiding in streamlined structure determination and mechanistic studies. The study was published in Acta Materia Medica by Yuan et al. (2024) and highlights the potential of AF2-mutation for protein tertiary structure prediction.
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