Sequential events in ribonuclease A thermal unfolding characterized by two-dimensional infrared correlation spectroscopy.
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.
Zhang
Jun
J
Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China.
He
Hua-Wei
HW
Wang
Qi
Q
Yan
Yong-Bin
YB
D002942:Circular Dichroism; D008958:Models, Molecular; D011487:Protein Conformation; D011489:Protein Denaturation; D012259:Ribonuclease, Pancreatic / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods*
D012259:Ribonuclease, Pancreatic