Nuclear magnetic resonance studies of the hydration of proteins and DNA.
The behaviour of water in the presence of proteins and DNA as elucidated by nuclear magnetic resonance is reviewed. The picture that emerges is that in dilute solution only those water molecules in the interior of the biopolymers or in clefts have their motions substantially affected. In concentrated systems the situation is more complicated because many more motions have to be considered, but there is no evidence of special effects due to the biopolymers being present. The case of nonfreezing water in protein solutions is considered, and it is suggested that this is not evidence for 'bound' water but simply due to the effects of the inhibition of protein precipitation.
Belton
P S
PS
Institute of Food Research, Norwich Research Park, Colney, United Kingdom. Peter.belton@bbsrc.ac.uk
D001704:Biopolymers / Q000737:chemistry / Q000378:metabolism; D004247:DNA / Q000737:chemistry / Q000378:metabolism*; D005615:Freezing; D009682:Magnetic Resonance Spectroscopy; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D011522:Protons; D012996:Solutions; D014867:Water / Q000737:chemistry / Q000378:metabolism*
D001704:Biopolymers; D011506:Proteins; D011522:Protons; D012996:Solutions; D014867:Water; D004247:DNA