Title of article :
Enzyme hydration, activity and flexibility: A neutron scattering approach
Author/Authors :
Kurkal-Siebert، نويسنده , , Vandana and Daniel، نويسنده , , R.M. and Finney، نويسنده , , John L. and Tehei، نويسنده , , M. and Dunn، نويسنده , , R.V. and Smith، نويسنده , , Jeremy C.، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2006
Pages :
7
From page :
4387
To page :
4393
Abstract :
Recent measurements have demonstrated enzyme activity at hydrations as low as 3%. The question of whether the hydration-induced enzyme flexibility is important for activity is addressed by performing picosecond dynamic neutron scattering experiments on pig liver esterase powders at various temperatures as well as solutions. At all temperatures and hydrations investigated here, significant quasielastic scattering intensity is found in the protein, indicating the presence of anharmonic, diffusive motion. As the hydration increases a temperature-dependent dynamical transition appears and strengthens involving additional diffusive motion. At low temperature, increasing hydration resulted in lower flexibility of the enzyme. At higher temperatures, systems containing sufficient number of water molecules interacting with the protein exhibit increased flexibility. The implication of these results is that, although the additional hydration-induced diffusive motion and flexibility at high temperatures in the enzyme detected here may be related to increased activity, they are not required for the enzyme to function.
Keywords :
biopolymers , Neutron diffraction/scattering , Hydration
Journal title :
Journal of Non-Crystalline Solids
Serial Year :
2006
Journal title :
Journal of Non-Crystalline Solids
Record number :
1380179
Link To Document :
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