ABSTRACT The WW domain consists of -40 residues, has no disulfide bridges, and forms a three-stranded antiparallel /-sheet that is monomeric in solution. It thus provides a model system for studying '-sheet stability in native proteins. We performed molecular dynamics simulations of two WW domains, YAP65 and FBP28, with very different stability characteristics, in order to explore the initial unfolding of thebeta/-sheet. The less stable YAP domain is much more sensitive to simulation conditions than the FBP domain. Under standard simulation conditions in water (with or without charge-balancing counterions) at 300 K, thebeta/-sheet of the YAP WW domain disintegrated at early stages of the …
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