TY - JOUR
T1 - Looking at hydrogen bonds in cellulose
AU - Nishiyama, Yoshiharu
AU - Langan, Paul
AU - Wada, Masahisa
AU - Forsyth, V. Trevor
PY - 2010/11
Y1 - 2010/11
N2 - A series of cellulose crystal allomorphs has been studied using high-resolution X-ray and neutron fibre diffraction to locate the positions of H atoms involved in hydrogen bonding. One type of position was always clearly observed in the Fourier difference map (Fd-Fh), while the positions of other H atoms appeared to be less well established. Despite the high crystallinity of the chosen samples, neutron diffraction data favoured some hydrogen-bonding disorder in native cellulose. The presence of disorder and a comparison of hydrogen-bond geometries in different allomorphs suggests that although hydrogen bonding may not be the most important factor in the stabilization of cellulose I, it is essential for stabilizing cellulose III, which is the activated form, and preventing it from collapsing back to the more stable cellulose I.
AB - A series of cellulose crystal allomorphs has been studied using high-resolution X-ray and neutron fibre diffraction to locate the positions of H atoms involved in hydrogen bonding. One type of position was always clearly observed in the Fourier difference map (Fd-Fh), while the positions of other H atoms appeared to be less well established. Despite the high crystallinity of the chosen samples, neutron diffraction data favoured some hydrogen-bonding disorder in native cellulose. The presence of disorder and a comparison of hydrogen-bond geometries in different allomorphs suggests that although hydrogen bonding may not be the most important factor in the stabilization of cellulose I, it is essential for stabilizing cellulose III, which is the activated form, and preventing it from collapsing back to the more stable cellulose I.
UR - http://www.scopus.com/inward/record.url?scp=78049483594&partnerID=8YFLogxK
U2 - 10.1107/S0907444910032397
DO - 10.1107/S0907444910032397
M3 - Article
C2 - 21041932
AN - SCOPUS:78049483594
SN - 0907-4449
VL - 66
SP - 1172
EP - 1177
JO - Acta Crystallographica Section D: Biological Crystallography
JF - Acta Crystallographica Section D: Biological Crystallography
IS - 11
ER -