Soluble structure of CLIC and S100 proteins investigated by atomic force microscopy

Valenzuela, S; Berkahn, MB; Porkovich, A; Huynh, TG; Goyette, J; Martin, DK; Geczy, CL

Soluble structure of CLIC and S100 proteins investigated by atomic force microscopy

Valenzuela, S

Berkahn, MB Porkovich, A Huynh, TG Goyette, J Martin, DK Geczy, CL

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Publisher:: Scientific Research Publishing
Publication Type:: Journal Article
Citation:: Journal of Biomaterials and Nanobiotechnology, 2011, 2 pp. 8 - 17
Issue Date:: 2011-01

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Field	Value	Language
dc.contributor.author	Valenzuela, S https://orcid.org/0000-0001-5934-6047	en_US
dc.contributor.author	Berkahn, MB	en_US
dc.contributor.author	Porkovich, A	en_US
dc.contributor.author	Huynh, TG	en_US
dc.contributor.author	Goyette, J	en_US
dc.contributor.author	Martin, DK	en_US
dc.contributor.author	Geczy, CL	en_US
dc.date.issued	2011-01	en_US
dc.identifier.citation	Journal of Biomaterials and Nanobiotechnology, 2011, 2 pp. 8 - 17	en_US
dc.identifier.issn	2158-7027	en_US
dc.identifier.uri	http://hdl.handle.net/10453/18337
dc.description.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.	en_US
dc.publisher	Scientific Research Publishing	en_US
dc.relation.ispartof	Journal of Biomaterials and Nanobiotechnology	en_US
dc.relation.isbasedon	10.4236/jbnb.2011.21002	en_US
dc.title	Soluble structure of CLIC and S100 proteins investigated by atomic force microscopy	en_US
dc.type	Journal Article
utslib.citation.volume	2	en_US
utslib.for	1007 Nanotechnology	en_US
utslib.for	0903 Biomedical Engineering	en_US
utslib.for	0912 Materials Engineering	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Life Sciences
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Medical and Molecular Sciences
pubs.organisational-group	/University of Technology Sydney/Strength - CHT - Health Technologies
pubs.organisational-group	/University of Technology Sydney/Strength - IBMD - Initiative for Biomedical Devices
utslib.copyright.status	closed_access
pubs.consider-herdc	true	en_US
pubs.publication-status	Published	en_US
pubs.volume	2	en_US

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.

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http://hdl.handle.net/10453/18337