Relation between the lysozyme hydration isotherm and molecule packing in the solid phase

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 i...

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Bibliographic Details
Published in:Biofizika Vol. 28; no. 6; p. 944
Main Authors: Gevorkian, S G, Morozov, V N
Format: Journal Article
Language:Russian
Published: Russia (Federation) 01-11-1983
Subjects:
Biophysical Phenomena
Biophysics
Crystallization
Macromolecular Substances
Muramidase
Ovalbumin
Temperature
Water
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Summary: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.
ISSN:0006-3029