Surfactant-Induced Amorphous Aggregation of Tobacco Mosaic Virus Coat Protein: A Physical Methods Approach

The interactions of non‐ionic surfactant Triton X‐100 and the coat protein of tobacco mosaic virus, which is an established model for both ordered and non‐ordered protein aggregation, were studied using turbidimetry, differential scanning calorimetry, isothermal titration calorimetry, and dynamic li...

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Veröffentlicht in:	Macromolecular bioscience 2008-02, Vol.8 (2), p.199-209
Hauptverfasser:	Panyukov, Yuliy V., Nemykh, Maria A., Dobrov, Eugeny N., Drachev, Vladimir A.
Format:	Artikel
Sprache:	eng
Schlagworte:	aggregation calorimetry Calorimetry, Differential Scanning Capsid Proteins - chemistry Chemistry, Physical - methods dynamic light scattering Micelles Nephelometry and Turbidimetry Octoxynol - chemistry proteins Sodium Dodecyl Sulfate - chemistry Surface-Active Agents - chemistry surfactants Tobacco mosaic virus Tobacco Mosaic Virus - chemistry
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