From shell to cell: neutron scattering studies of biological water dynamics and coupling to activity.
An integrated picture of hydration shell dynamics and of its coupling to functional macromolecular motions is proposed from studies on a soluble protein, on a membrane protein in its natural lipid environment, and on the intracellular environment in bacteria and red blood cells. Water dynamics in multimolar salt solutions was also examined, in the context of the very slow water component previously discovered in the cytoplasm of extreme halophilic archaea. The data were obtained from neutron scattering by using deuterium labelling to focus on the dynamics of different parts of the complex systems examined.
Frölich
A
A
Institut de Biologie Structurale, UMR 5075, CEA-CNRS-UJF, Grenoble, France.
Gabel
F
F
Jasnin
M
M
Lehnert
U
U
Oesterhelt
D
D
Stadler
A M
AM
Tehei
M
M
Weik
M
M
Wood
K
K
Zaccai
G
G
D001436:Bacteriorhodopsins / Q000737:chemistry; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism; D002448:Cell Adhesion / Q000502:physiology; D003593:Cytoplasm / Q000737:chemistry / Q000378:metabolism; D003903:Deuterium / Q000737:chemistry; D004912:Erythrocytes / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D019614:Haloarcula marismortui / Q000378:metabolism; D058619:Maltose-Binding Proteins; D008563:Membrane Lipids / Q000737:chemistry; D033363:Neutron Diffraction; D018717:Purple Membrane / Q000737:chemistry / Q000378:metabolism; D012492:Salts / Q000737:chemistry; D012995:Solubility; D012996:Solutions / Q000737:chemistry; D013696:Temperature; D014867:Water / Q000737:chemistry* / Q000378:metabolism; D017155:Wettability
D002352:Carrier Proteins; D058619:Maltose-Binding Proteins; D008563:Membrane Lipids; D012492:Salts; D012996:Solutions; D014867:Water; D001436:Bacteriorhodopsins; D003903:Deuterium