Can grafting of an octapeptide improve the structure of a de novo protein?

Structural properties and conformational stability of de novo proteins – albebetin and albeferon (albebetin with a grafted interferon fragment) – were studied by means of CD spectroscopy, gel filtration and urea-induced unfolding. The results allow us to conclude that albebetin possesses the propert...

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Bibliographic Details
Published in:	FEBS letters Vol. 425; no. 1; pp. 101 - 104
Main Authors:	Aphasizheva, Inna Yu, Dolgikh, Dmitry A, Abdullaev, Ziedulla K, Uversky, Vladimir N, Kirpichnikov, Mikhail P, Ptitsyn, Oleg B
Format:	Journal Article
Language:	English
Published:	England Elsevier B.V 20-03-1998
Subjects:	Chromatography, Gel Circular Dichroism Cloning, Molecular De novo protein Escherichia coli - genetics Interferon Molten globule Oligopeptides - chemistry Protein design Protein Engineering Protein expression Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Proteins - chemistry Proteins - genetics Recombinant Proteins - chemistry Recombinant Proteins - genetics Thermodynamics Urea - chemistry Protein expression Interferon De novo protein Protein design Molten globule
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Summary:	Structural properties and conformational stability of de novo proteins – albebetin and albeferon (albebetin with a grafted interferon fragment) – were studied by means of CD spectroscopy, gel filtration and urea-induced unfolding. The results allow us to conclude that albebetin possesses the properties of the molten globule state. Grafting of the octapeptide to the N-terminus of this de novo protein affects its structure. We show here that albeferon maintains a secondary structure content of albebetin; it becomes more compact and much more stable toward urea-induced unfolding as compared to albebetin and even possesses some weak tertiary structure (at least around Tyr 7). This means that the structure of the artificial protein albebetin can be improved by a simple procedure of octapeptide grafting to its N-terminus.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0014-5793 1873-3468
DOI:	10.1016/S0014-5793(98)00201-4