Aphasizheva I Y, Dolgikh D A, Abdullaev Z K, Uversky V N, Kirpichnikov M P, Ptitsyn O B
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow.
FEBS Lett. 1998 Mar 20;425(1):101-4. doi: 10.1016/s0014-5793(98)00201-4.
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 Tyr7). This means that the structure of the artificial protein albebetin can be improved by a simple procedure of octapeptide grafting to its N-terminus.
通过圆二色光谱、凝胶过滤和尿素诱导的去折叠研究了从头合成蛋白质——albetein和albeferon（带有嫁接干扰素片段的albetein）的结构特性和构象稳定性。结果使我们能够得出结论，albetein具有熔球态的性质。八肽嫁接到这种从头合成蛋白质的N端会影响其结构。我们在此表明，albeferon保持了albetein的二级结构含量；与albetein相比，它变得更加紧凑，对尿素诱导的去折叠更稳定，甚至具有一些弱的三级结构（至少在Tyr7周围）。这意味着通过将八肽嫁接到其N端的简单程序可以改善人工蛋白质albetein的结构。
