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

被引：14

作者：

Aphasizheva, IY ^{[1
]}

Dolgikh, DA

Abdullaev, ZK

Uversky, VN

Kirpichnikov, MP

Ptitsyn, OB

机构：

[1] Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow 117871, Russia

[2] Russian Acad Sci, Inst Prot Res, Pushchino 142292, Moscow Region, Russia

[3] NCI, Lab Expt & Computat Biol, NIH, Bethesda, MD 20892 USA

来源：

FEBS LETTERS | 1998年 / 425卷 / 01期

关键词：

de novo protein; molten globule; protein expression; protein design; interferon;

D O I：

10.1016/S0014-5793(98)00201-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 1998 Federation of European Biochemical Societies.

引用

页码：101 / 104

页数：4

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