Sequential events in ribonuclease A thermal unfolding characterized by two-dimensional infrared correlation spectroscopy.

Academic Article


  • The conformational changes in the thermal denaturation of bovine pancreatic ribonuclease A was followed with infrared spectra and analyzed by second derivative and two-dimensional correlation techniques. By analyzing the sequential events in each transition stage, the results were consistent with a step-wise thermal denaturation mechanism in which the structural adjustment of the N-terminal and the opening of the central structure of the protein come before the main unfolding process. Non-native turns were found to form along with the unfolding of the native structures. The central region that is composed of some beta-sheet and alpha-helical structures was found to be the most stable part that might form the residual structure at high temperatures.
  • Authors


  • Circular Dichroism, Models, Molecular, Protein Conformation, Protein Denaturation, Ribonuclease, Pancreatic, Spectroscopy, Fourier Transform Infrared
  • Digital Object Identifier (doi)

    Author List

  • Zhang J; He H-W; Wang Q; Yan Y-B
  • Start Page

  • 33
  • End Page

  • 40
  • Volume

  • 13
  • Issue

  • 1