Hydration structures in proteins and neutron diffraction experiment on dissimilatory sul te reductase D (DsrD).
Neutron crystallography can provide a substantial amount of information about the hydration of proteins. The hydration patterns of three proteins, whose structures have been solved at 1.5 or 1.6 A resolution using our BIX-type diffractometers, show interesting features. The water molecules adopt a variety of shapes in the neutron Fourier maps, revealing details of intermolecular hydrogen-bond formation and dynamics of hydration. In addition, the neutron diffraction study of a DNA-binding protein, dissimilatory sulfite reductase D (DsrD) is briefly described, and some preliminary results are presented. This topic is of interest because it is well known that hydrogen bonds play important roles in DNA-protein recognition.
Chatake
Toshiyuki
T
Neutron Structural Biology, Neutron Science Research Center, Japan Atomic Energy Research Institute, Tokai, Ibaraki 319-1195, Japan.
Ostermann
Andreas
A
Kurihara
Kazuo
K
Parak
Fritz G
FG
Mizuno
Nobuhiro
N
Voordouw
Gerrit
G
Higuchi
Yoshiki
Y
Tanaka
Ichiro
I
Niimura
Nobuo
N
D001665:Binding Sites; D006860:Hydrogen Bonding; D046911:Macromolecular Substances; D009211:Myoglobin / Q000737:chemistry*; D033363:Neutron Diffraction / Q000379:methods*; D050862:Oxidoreductases Acting on Sulfur Group Donors / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D012416:Rubredoxins / Q000737:chemistry*; D012680:Sensitivity and Specificity; D014867:Water / Q000737:chemistry*
D046911:Macromolecular Substances; D009211:Myoglobin; D012416:Rubredoxins; D014867:Water; D050862:Oxidoreductases Acting on Sulfur Group Donors