Predicting binding events in very flexible, allosteric, multi-domain proteins
A. Basciu, M. Athar, H. Kurt, C. Neville, G. Malloci, F. Muredda, A. Bosin, P. Ruggerone, A. Bonvin, A. V. Vargiu
This paper introduces a method to generate bound-like conformations of flexible, multi-domain proteins using unbound structures and binding site information, demonstrating its effectiveness on adenylate kinase.
bioRxiv · Jun 2, 2024Biophysics