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Denaturation studies of P2 protein using circular dichroism.

Barbara H. Stuart

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Abstract

The denaturation process of P2 protein has been investigated using circular dichroism spectroscopy. The influence of temperature and the presence of urea were the factors investigated. Increasing temperature causes the destruction of beta-structure, while helical structure remains intact even at relatively high temperatures. Increasing the urea concentration destroyed all forms of secondary structure in P2 and the study also supports the model of a stepwise denaturation process of the protein.

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The denaturation process of P2 protein has been investigated using circular dichroism spectroscopy. The influence of temperature and the presence of urea were the factors investigated. Increasing temperature causes the destruction of beta-structure, while helical structure remains intact even at relatively high temperatures. Increasing the urea concentration destroyed all forms of secondary structure in P2 and the study also supports the model of a stepwise denaturation process of the protein.

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Available abstract

The denaturation process of P2 protein has been investigated using circular dichroism spectroscopy. The influence of temperature and the presence of urea were the factors investigated. Increasing temperature causes the destruction of beta-structure, while helical structure remains intact even at relatively high temperatures. Increasing the urea concentration destroyed all forms of secondary structure in P2 and the study also supports the model of a stepwise denaturation process of the protein.

Key concepts: Circular dichroism, Denaturation (fissile materials), Urea, Protein secondary structure, Chemistry, Crystallography, Protein structure, Biophysics

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