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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1986 Jun;83(12):4268–4272. doi: 10.1073/pnas.83.12.4268

Role of conformational changes in the elution of proteins from reversed-phase HPLC columns.

G E Katzenstein, S A Vrona, R J Wechsler, B L Steadman, R V Lewis, C R Middaugh
PMCID: PMC323713  PMID: 3459173

Abstract

To test the hypothesis that conformational alterations might be involved in the elution of proteins from reversed-phase HPLC columns, the conformations of proteins bound onto a C-8 alkyl-bonded silica surface have been examined in the presence of increasing concentrations of the commonly employed eluent, 1-propanol. Using a combination of photoacoustic, diffuse reflectance deconvolution Fourier transform infrared and front face fluorescence spectroscopic techniques (to minimize interference from light scattering), the existence of surface-associated protein conformational changes induced by propanol is unequivocally demonstrated. The linear relationship found between the amount of propanol needed to elute proteins from C-8 columns and the midpoint of spectrally observed structural transitions is consistent with a role for conformational changes in the elution process.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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