Shang, Wen and Nuffer, Joseph H. and Dordick, Jonathan S. and Siegel, Richard W. (2007) Unfolding of ribonuclease A on silica nanoparticle surfaces. NANO LETTERS, 7 (7). pp. 1991-1995.
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Official URL: http://dx.doi.org/10.1021/nl070777r
This paper reports on the unfolding behavior of ribonuclease A (RNase A) on silica nanoparticle surfaces and quantitively demonstrates that nanoscale size and surface curvature play key roles in influencing the stability of adsorbed proteins. Urea denaturation analyses showed that the thermodynamic stability of RNase A decreased upon adsorption onto the nanoparticles, with greater decrease on larger nanoparticles. The stability changes of RNase A correlate well with the changes in the protein-nanoparticle interactions, which increase as the surface contact area and surface charge interaction increases. This study, therefore, provides fundamental information on the effect of nanoscale surfaces on protein structure and function.
|Subjects:||Physical Science > Nano objects|
Biomedical Science > Nanobiotechnology
|Deposited By:||Anuj Seth|
|Deposited On:||18 Dec 2008 16:28|
|Last Modified:||20 Jan 2009 10:43|
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