Use of high-performance size-exclusion, ion-exchange, and hydrophobic interaction chromatography for the measurement of protein conformational change and stability.


Size-exclusion, ion-exchange, and hydrophobic interaction chromatographic techniques able to detect conformational changes induced by urea were developed for three globular proteins: bovine serum albumin, lysozyme, and trypsin. Alterations in tertiary structure were manifest chromatographically by highly reproducible changes in peak height, retention, and… (More)


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