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Soluble Structure of CLIC and S100 Proteins Investigated by Atomic Force Microscopy

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DOI: 10.4236/jbnb.2011.21002    5,442 Downloads   8,940 Views   Citations

ABSTRACT

The ability to visualise proteins in their native environment and discern information regarding stoichiometry is of critical importance when studying protein interactions and function. We have used liquid cell atomic force microscopy (AFM) to visualise proteins in their native state in buffer and have determined their molecular volumes. The human proteins S100A8, S100A9, S100A12 and CLIC1 were used in this investigation. The effect of oxidation on the protein structure of CLIC1 was also investigated and we found that CLIC1 multimerisation could be discerned by AFM, which supports similar findings by other methods. We have found good correlation between the molecular volumes measured by AFM and the calculated volumes of the individual proteins. This method allows for the study of single soluble proteins under physiological conditions and could potentially be extended to study the structure of these proteins when located within a membrane environment.

Conflicts of Interest

The authors declare no conflicts of interest.

Cite this paper

S. Valenzuela, M. Berkahn, A. Porkovich, T. Huynh, J. Goyette, D. Martin and C. Geczy, "Soluble Structure of CLIC and S100 Proteins Investigated by Atomic Force Microscopy," Journal of Biomaterials and Nanobiotechnology, Vol. 2 No. 1, 2011, pp. 8-17. doi: 10.4236/jbnb.2011.21002.

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