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

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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; H/D exchange; infrared; thermal stability; two-dimensional correlation spectroscopy

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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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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