The response of c-terminal variants of ribonuclease a to pressure and temperature-induced unfolding. A study by fourth derivative UV and Fourier Transform Infrared spectroscopy

J. Torrent University of Girona, Faculty of Sciences, Department of Biology, Protein Engineering Laboratory, Campus de Montilivi, E-17071, Girona, Spain

J. P. Connelly INSERM U128, IFR 24, 1919 Route de Mende, F-34293, Montpellier, France

P. Rubens Katholieke Universiteit Leuven, Department of Chemistry, Celestijnenlaan 200 D, B-3001, Leuven, Belgium

M. G. Coll University of Girona, Faculty of Sciences, Department of Biology, Protein Engineering Laboratory, Campus de Montilivi, E-17071, Girona, Spain

M. RibÓ University of Girona, Faculty of Sciences, Department of Biology, Protein Engineering Laboratory, Campus de Montilivi, E-17071, Girona, Spain

R. Lange INSERM U128, IFR 24, 1919 Route de Mende, F-34293, Montpellier, France

K. Heremans Katholieke Universiteit Leuven, Department of Chemistry, Celestijnenlaan 200 D, B-3001, Leuven, Belgium

M. Vilanova University of Girona, Faculty of Sciences, Department of Biology, Protein Engineering Laboratory, Campus de Montilivi, E-17071, Girona, Spain

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Abstract

The effect of pressure and temperature on ribonuclease A WT and a set of variants was studied by fourth derivative UV and Fourier Transform Infrared spectroscopy. The results reveal an unusual similarity between pressure- and temperature-induced unfolding and indicate the importance of the region extending from residue 106 to 118 (of 124) in stability and probably in the early stages of folding.

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The response of c-terminal variants of ribonuclease a to pressure and temperature-induced unfolding. A study by fourth derivative UV and Fourier Transform Infrared spectroscopy

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The response of c-terminal variants of ribonuclease a to pressure and temperature-induced unfolding. A study by fourth derivative UV and Fourier Transform Infrared spectroscopy

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