Spectroscopic study of the temperature-dependent conformation of glucoamylase

  • Urbanova M
  • Pancoska P
  • Keiderling T
  • 3


    Mendeley users who have this article in their library.
  • 34


    Citations of this article.


Vibrational circular dichroism, electronic circular dichroism and infrared absorption with Fourier self-deconvolution have been used for a coformational study of the small form, G2, of glucoamylase, 1,4-α-d-glucan glucohydrolase from Aspergillus niger (EC in aqueous solution. From the temperature dependence of spectra measured from 25°C to 60°C it was seen that the helical content is relatively constant to 50°C and then sharply decreases by a factor of more than three by 60°C. This decrease in helix is primarily compensated by a rise in the fraction of β-sheet; but bend, turn and 'other' components also increase. By comparison of the three techniques, it was determined that the electric CD analysis was quantitatively in error due to interference by glycosidic residues. The inherent resolution of the vibrational techniques, FTIR and VCD, avoids such interference. © 1993.

Author-supplied keywords

  • Circular dichroism
  • Glucoamylase G2
  • Infrared spectroscopy
  • Protein conformation

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document


  • Marie Urbanova

  • Petr Pancoska

  • Timothy A. Keiderling

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free