Stability check of succinylated concanavalin A: presence of functionally active conformational state

Protein Pept Lett. 2009;16(4):423-9. doi: 10.2174/092986609787848117.

Abstract

The equilibrium denaturation pathway of Succinyl Con A exhibited three-state mechanism with the transition midpoints at 1 and 3 M GdnHCl and at 2.6 and 5 M urea. Unfolding resulted in stabilization of molten-globule (MG) like intermediate states at 2 M GdnHCl and 3 M urea. It was particularly interesting that state obtained at 3 M urea was functionally active.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Concanavalin A / chemistry*
  • Guanidine / pharmacology
  • Hot Temperature
  • Protein Conformation / drug effects*
  • Protein Denaturation
  • Protein Folding / drug effects
  • Protein Multimerization
  • Protein Stability
  • Spectrometry, Fluorescence
  • Urea / pharmacology

Substances

  • Concanavalin A
  • succinylconcanavalin A
  • Urea
  • Guanidine