Atomic structure of a glycerol channel and implications for substrate permeation in aqua(glycero)porins.
The slide was mounted with 50 % glycerol and examined under a fluorescent microscope.
Selectivity and conductance among the glycerol and water conducting aquaporin family of channels.
For two compounds (glycerol and glyceric acid) abundances were determined on the same order of magnitude as for the amino acid glycine.
The authors drew the conclusion that glycerol facilitated, even though not to the same degree of water, the anharmonic transition in proteins.
Lipid hydrolysis was also detected by measuring lipase activity with glycerol ester as substrate.
When diapause is completed, the concentration of cryoprotectors (for example, glycerol) and tolerance of low temperatures decline significantly, even under constant external temperature conditions.
Bioprotectants such as glycerol and trehalose as well as organic solvents have been used in experiments with lyophilized protein powders.
