Structural Stability of Globulins

Shela Gorinstein*, Marina Zemser, Octavio Paredes-López

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

51 Scopus citations

Abstract

Application of differential scanning calorimetry (DSC) and the susceptibility of amaranth globulins (A-G) to α-chymotrypsin gave a quantitative estimation of protein denaturation in solid state. To compare effects of size and crystal structure, A-G, quinoa globulins (Q-G), and bovine γ-globulins (γ-G) were examined at similar conditions for the extent of denaturation. A-G and Q-G showed similar data, but γ-G exhibited maximal conformational changes. The larger percentage of denaturation in globulins that is associated with enthalpy and the number of ruptured hydrogen bonds correspond to the smaller crystallinity determined by X-ray diffraction and disappearance of the α-helix in Fourier transform-infrared spectra.

Original languageEnglish
Pages (from-to)100-105
Number of pages6
JournalJournal of Agricultural and Food Chemistry
Volume44
Issue number1
DOIs
StatePublished - Jan 1996

Keywords

  • Amaranth
  • Calorimetry
  • Denaturation
  • Quinoa
  • Spectroscopy

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