Investigation of the conformation of d-glyceraldehyde-3-phosphate dehydrogenase

I. A. Bolotina, D. S. Markovich, M. V. Volkenstein, P. Zavodsky

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The conformation of d-glyceraldehyde-3-phosphate dehydrogenase was studied by means of spectropolarimetry under various conditions. It was shown that at neutral pH the enzyme possesed a compact globular structure with approx. 40% α-helical content. When the pH was altered, a change in secondary and tertiary structure was observed which was manifested in the change of α-helicity and in the uncoiling of the molecules. Sodium dodecylsulphate produced a change in the tertiary and quaternary structure, i.e. uncoiling of the molecules and the division of the enzyme molecule into subunits, while the secondary structure remained unchanged. The coenzyme (NAD+) and the substrate (glyceraldehyde) produced conformational changes in the apoenzyme molecule. The results can be interpreted in terms of Koshland's "induced-fit" hypothesis.

Original languageEnglish
Pages (from-to)260-270
Number of pages11
JournalBBA - Enzymology
Issue number2
Publication statusPublished - Mar 15 1967

ASJC Scopus subject areas

  • Medicine(all)

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