Direct measurement of the viscoelasticity of adsorbed protein layers using atomic force microscopy.
Thick layers of the protein lysozyme have been deposited on mica, and their force-distance hysteresis measured using atomic force microscopy in the presence of different salts. Sodium thiocyanate, which is known to lower the melting temperature of proteins and increase their solubility, increases lysozyme deformability and lowers the viscosity of the protein layer, compared with sodium chloride. Sodium phosphate, known to raise the melting temperature and lower the solubility, decreases deformability and increases the viscosity.
Nemes
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Department of Biological Physics, Eötvös University, Pázmány P. sétány 1/A, 1117 Budapest, Hungary.
Rozlosnik
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Ramsden
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D000818:Animals; D002645:Chickens; D018625:Microscopy, Atomic Force / Q000379:methods*; D009113:Muramidase / Q000737:chemistry*; D010710:Phosphates / Q000494:pharmacology; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D012965:Sodium Chloride / Q000494:pharmacology; D013696:Temperature; D014783:Viscosity
D010710:Phosphates; D011506:Proteins; D012965:Sodium Chloride; D009113:Muramidase; C018279:sodium phosphate