2006
DOI: 10.1016/j.ab.2006.01.008
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Secondary structures of proteins adsorbed onto aluminum hydroxide: Infrared spectroscopic analysis of proteins from low solution concentrations

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Cited by 70 publications
(52 citation statements)
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“…Previous studies reported that IR spectra of the protein adsorbed to alum show native structure. 27 Therefore, we assume that mGH adsorbed to alum has native secondary structure. In previous circular dichroism analysis of the monomeric mGH, we reported that the protein contained 60% "-helix.…”
Section: Analysis Of Mgh Secondary Structure In Aggregates and Adsorbmentioning
confidence: 99%
“…Previous studies reported that IR spectra of the protein adsorbed to alum show native structure. 27 Therefore, we assume that mGH adsorbed to alum has native secondary structure. In previous circular dichroism analysis of the monomeric mGH, we reported that the protein contained 60% "-helix.…”
Section: Analysis Of Mgh Secondary Structure In Aggregates and Adsorbmentioning
confidence: 99%
“…10 A number of biophysical analyses specifically looking at the structure of model antigens bound to aluminum based hydrated gels, have revealed none or subtle effects upon the bound protein. [11][12][13][14][15][16] Even though alum adjuvantation is not expected to affect the properties of Sm-Tsp-2, future studies will be able to address and document that this indeed is the case.…”
Section: Introductionmentioning
confidence: 99%
“…Structural studies have shown that Alhydrogel-bound proteins, including rPA, preserve their secondary (19,20), tertiary (18), and quaternary (21,22) structures but exhibit decreased thermal stability, compared to their free counterparts in solution (23,24). At the surfaces of adjuvant particles, bound proteins form a monolayer in which individual biomolecules are packed closely together, with no apparent preference for any particular surface orientation.…”
mentioning
confidence: 99%