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Can grafting of an octapeptide improve the structure of a de novo protein?
Author(s) -
Aphasizheva Inna Yu,
Dolgikh Dmitry A,
Abdullaev Ziedulla K,
Uversky Vladimir N,
Kirpichnikov Mikhail P,
Ptitsyn Oleg B
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00201-4
Subject(s) - urea , chemistry , grafting , protein tertiary structure , size exclusion chromatography , protein structure , protein secondary structure , biophysics , crystallography , native state , biochemistry , biology , enzyme , organic chemistry , polymer
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.