Phage tailspike proteins with beta-solenoid fold as thermostable carbohydrate binding materials.
Phage tailspike proteins with beta-solenoid fold as thermostable carbohydrate binding materials.
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具有β-螺线管折叠的噬菌体尾刺蛋白作为热稳定性碳水化合物结合材料。
DOI：
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发表时间：
2009
影响因子：
4.6
通讯作者：
R. Seckler
中科院分区：
文献类型：
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作者：
S. Barbirz;M. Becker;Alexander N. Freiberg;R. Seckler
我们研究了来自噬菌体SF6、P22和HK620的三种尾尖蛋白(TSP)的稳定性。尾钉是杆状三聚体，具有类似的β-螺线管折叠和类似的高动力学稳定性，尽管氨基酸序列不同。由于尾刺结合多糖识别细菌宿主细胞，它们的稳定性是在严酷的细胞外条件下保持噬菌体感染性所必需的。它们在常温下抵抗十二烷基硫酸钠的变性，即使在6M盐酸胍(GdmHCl)中，它们的折叠也很慢。这使它们成为非常稳定的碳水化合物结合蛋白材料的有趣候选者。
We have investigated the stability of three tailspike proteins (TSPs) from bacteriophages Sf6, P22, and HK620. Tailspikes are rod-like homotrimers with comparable beta-solenoid folds and similarly high kinetic stability in spite of different amino acid sequences. As tailspikes bind polysaccharides to recognize the bacterial host cell, their stability is required for maintenance of bacteriophage infectivity under harsh extracellular conditions. They resist denaturation by SDS at ambient temperature and their unfolding is slow even in 6 M guanidinium hydrochloride (GdmHCl). This makes them interesting candidates for very stable carbohydrate binding protein materials.
影响因子：
2.9
作者：
CHEN, BL;KING, J
通讯作者：
KING, J
P22 尾刺蛋白温度敏感折叠突变体的热稳定性。
DOI：
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发表时间：
1989
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Sturtevant,JM;Yu,MH;Haase-Pettingell,C;King,J
通讯作者：
King,J