For specifically the interaction of surfactants on protein folding, this might be a good place to start.

Protein–surfactant interactions: A tale of many states

http://www.sciencedirect.com/science/article/pii/S1570963911000549

First, are you working with membrane proteins or globular proteins?

Second, its typically best to use too different spectroscopic techniques that probe different structural aspects of the protein during folding, for instance uv-vis and fluorescence.

The Classical Fersht book gives you a good, and still up to date, guide in protein folding both from an experimental and theoretical point of view. (Structure and mechanism in protein science by Alan Fersht)

CD and fluorescence spectroscopy are usually preferable methods than UV/Vis to monitor protein folding/unfolding. For information about UV/Vis, CD, and fluorescence spectroscopy, I suggest a general review I wrote: Colon, W. Analysis of protein structure by solution spectroscopy. Methods Enzymol. 310, 316-340 (1999). You may download it from my pubs list here or e-mail me and I'll send it to you.

When we speak of surfactants, we often have to deal with cloudy solutions that prevent the use of several spectroscopic techniques because of the high and turbid background. In these cases I suggest the use of derivative spectroscopy, developed by my group in the eighties, which is not affected much by the turbidity of the solutions because the linear increase of the background is canceled in its second derivative and you can follow the exposure of tyrosines as well as tryptophan.

dear Wilfredo Colón

i could not find the review whatever you suggested, could you please send the review to my mail. for which i am thankful to you.

mail : [email protected]