Conformational changes in proteins caused by surfactants.
نویسندگان
چکیده
منابع مشابه
Measuring Surface-Induced Conformational Changes in Proteins
Microfabricated cantilever sensors were used to measure the surface stress induced by protein adsorption onto a gold surface. Two proteins, immoglobulin G (IgG) and albumin (BSA), were studied. The change of surface stress upon adsorption of IgG was found to be compressive, whereas that of BSA was tensile. This difference is elucidated in terms of protein deformation and packing. Most stress ch...
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Liquid protein formulations are prone to form aggregates. The effect of nonionic surfactants such as Polysorbate 20 (PS 20) and n-Dodecyl β-D-maltoside (DDM) on the prevention of aggregation and conformational changes of recombinant human IFNβ-1b (rhIFN β_1b) was explored. Polysorbate has been used in formulations of protein pharmaceuticals. There have been concerns about using PS 20 due to its...
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Liquid protein formulations are prone to form aggregates. The effect of nonionic surfactants such as Polysorbate 20 (PS 20) and n-Dodecyl β-D-maltoside (DDM) on the prevention of aggregation and conformational changes of recombinant human IFNβ-1b (rhIFN β_1b) was explored. Polysorbate has been used in formulations of protein pharmaceuticals. There have been concerns about using PS 20 due to its...
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The reactivity of protein thiol groups in human lens and the susceptibility of the proteins to tryptic digestion were investigated. Both were found to be greater in some cataractous lenses, indicating that lens proteins have unfolded during cataractogenesis. Almost all the tyrosine in the proteins of the normal human lens reacts with tetranitromethane and is therefore probably on the outside of...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 1990
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.30.1