Sequential Events in Ribonuclease A Thermal Unfolding Characterized by Two-Dimensional Infrared Correlation Spectroscopy

Author(s): J. Zhang, H.- W. He, Q. Wang, Y.- B. Yan.

Journal Name: Protein & Peptide Letters

Volume 13 , Issue 1 , 2006

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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 β-sheet and α-helical structures was found to be the most stable part that might form the residual structure at high temperatures.

Keywords: Bovine pancreatic ribonuclease A,, infrared, thermal stability, two-dimensional correlation spectroscopy, H/D exchange

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Article Details

Year: 2006
Page: [33 - 40]
Pages: 8
DOI: 10.2174/092986606774502027

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