| Comments |
P.181 left column bottom paragraph: "In agreement with the expectations based on volume exclusion [ref 109], the influence of such crowding environment in terms of thermodynamic stability of a protein has been reported by various researchers (Table 1). Batra and co-workers have shown that among different sizes of dextran (6, 10, 20, 40, 70, 100 and 150 kDa) and ficoll 70, the maximum stabilization of FK-506 binding protein (FKBP) in terms of unfolding free energy was found at 100 g/l of 40 kDa signifying that both size and concentration of a crowder are worth taking into consideration [primary source 30]." |