[Relation between the lysozyme hydration isotherm and molecule packing in the solid phase].
A micromethod for measurement of mass changes of glutaraldehyde treated protein crystals is presented. The method is based on analysis of transverse resonance vibration of a cantilevered tungsten micro-needle (1,5 divided by 2 mm long, 30 divided by 40 mkm in diameter) having the specimen stuck on its free sharp end. The method is accurate to within 0.1% for specimens with masses 0.1 divided by 0.01 mg. Absorption isotherms for water uptake by triclinic (P1), monoclinic (P2(1) ) and tetragonal (P4(3)2(1)2) crystals as well as by amorphous films of hen egg-white lysozyme are obtained. Hydration of lysozyme molecule is shown to be highly dependent on molecular packing in the sample both at low and high relative humidities.
D055592:Biophysical Phenomena; D001703:Biophysics; D003460:Crystallization; D046911:Macromolecular Substances; D009113:Muramidase; D010047:Ovalbumin; D013696:Temperature; D014867:Water
D046911:Macromolecular Substances; D014867:Water; D010047:Ovalbumin; D009113:Muramidase
Zavisimost' izotermy gidratatsii lizotsima ot upakovki molekul v tverdoĭ faze.