NDLI: Oligomerization of hydrophobin SC3 in solution: From soluble state to self-assembly

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Oligomerization of hydrophobin SC3 in solution: From soluble state to self-assembly

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Oligomerization of hydrophobin SC3 in solution: From soluble state to self-assembly

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Graveland-Bikker, Johanna F. Robillard, George T. Wang, Xiaoqin de Kruif, Cornelis G.
Description	Country affiliation: Netherlands Author Affiliation: Wang X ( BioMaDe Technology Foundation, and Department of Biochemistry, University of Groningen, 9747 AG Groningen, The Netherlands.)
Abstract	Hydrophobin SC3 is a protein with special self-association properties that differ depending on whether it is in solution, on an air/water interface or on a solid surface. Its self-association on an air/water interface and solid surface have been extensively characterized. The current study focuses on its self-association in water because this is the starting point for the other two association processes. Size-exclusion chromatography was used to fractionate soluble-state SC3. Real-time multiangular light scattering detection of the eluate indicated that SC3 mainly exists as a dimer in buffer, accompanied with a small amount of monomer, tetramer, and larger aggregates. Dimeric SC3 has very likely an elongated shape, as indicated by the hydrodynamic radius determined by using dynamic light scattering (DLS) and fluorescence anisotropy measurements on dansyl-labeled SC3. Size-exclusion chromatography experiments also indicated that the protein oligomerizes very slowly at low temperature (4 degrees C) but rather rapidly at room temperature. Ionic strength plays an important role in the oligomerization; a short-lived monomeric SC3 species could be observed in pure water. Oligomerization was not affected by low pH but was accelerated by high pH. Fluorescence resonance energy transfer showed that dissociation occurred when the protein concentration was lowered; a large population of oligomers, presumably dimers, dissociate when the protein concentration is <4.5 microg/mL. This value is similar to the critical concentration for SC3 self-assembly. Therefore, dimeric SC3 is indicated to be the building block for both aggregation in solution and self-assembly at hydrophobic/hydrophilic interfaces.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	3
Volume Number	13
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2004-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Fungal Proteins Chemistry Chromatography, Gel Chromatography, High Pressure Liquid Circular Dichroism Fluorescence Resonance Energy Transfer Fluorescent Dyes Metabolism Hydrogen-ion Concentration Models, Chemical Nuclear Magnetic Resonance, Biomolecular Osmolar Concentration Protein Binding Protein Conformation Scattering, Radiation Solubility Spectrometry, Fluorescence Trifluoroacetic Acid Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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