Sequential Events in Ribonuclease A Thermal Unfolding Characterized by Two-Dimensional Infrared Correlation Spectroscopy
Abstract: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.
Document Type: Research Article
Affiliations: Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China.
Publication date: January 1, 2006
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