Inactivation during denaturation of ribonuclease A by guanidinium chloride is accompanied by unfolding at the active site.

Lignende værker

• Comparison of the activity and conformation changes of lactate dehydrogenase H4 during denaturation by guanidinium chloride.
  af: Ma, Y Z, et al.
  Udgivet: (1991)
• Inactivation precedes changes in allosteric properties and conformation of D-glyceraldehyde-3-phosphate dehydrogenase and fructose-1,6-bisphosphatase during denaturation by guanidinium chloride.
  af: Jiang, R F, et al.
  Udgivet: (1994)
• Cooperative Unfolding of Residual Structure in Heat Denatured Proteins by Urea and Guanidinium Chloride
  af: Singh, Ritu, et al.
  Udgivet: (2015)
• Conformational changes at the active site of creatine kinase at low concentrations of guanidinium chloride.
  af: Zhou, H M, et al.
  Udgivet: (1993)
• Dissociation and unfolding of the pyruvate dehydrogenase complex by guanidinium chloride.
  af: West, S M, et al.
  Udgivet: (1995)