Chimeras of human lysozyme and α-lactalbumin: an interesting tool for studying partially folded states during protein folding |
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Authors: | H Van Dael |
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Institution: | (1) Interdisciplinary Research Centre, K. U. Leuven Campus Kortrijk, B-8500 Kortrijk (Belgium), Fax +32 56 246997, e-mail: Herman.Vandael@kulak.ac.be, BE |
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Abstract: | Protein folding is an extremely active field of research where biology, chemistry, computer science and physics meet. Although
the study of protein-folding intermediates in general and equilibrium intermediates in particular has grown considerably in
recent years, many questions regarding the conformational state and the structural features of the various partially folded
intermediate states remain unanswered. Performing kinetic measurements on proteins that have had their structures modified
by site-directed mutagenesis, the so-called protein-engineering method, is an obvious way to gain fine structural information.
In the present review, this method has been applied to a variety of proteins belonging to the lysozyme/α-lactalbumin family. Besides recombinants obtained by point mutations of individual critical residues, chimeric proteins in
which whole structural elements (10 – 25 residues) from α-lactalbumin were inserted into a human lysozyme matrix are examined. The conformational properties of the equilibrium intermediate
states are discussed together with the structural characterization of the partially unfolded states encountered in the kinetic
folding pathway.
Received 28 May 1998; received after revision 6 July 1998; accepted 6 July 1998 |
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Keywords: | , Lysozyme, molten globule, protein folding, α,-lactalbumin, folding intermediates, protein engineering, chimera,,,,,,stability, |
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