SCANNING TUNNELING MICROSCOPY OF A WHEAT SEED STORAGE PROTEIN REVEALS DETAILS OF AN UNUSUAL SUPERSECONDARY STRUCTURE
SCANNING TUNNELING MICROSCOPY OF A WHEAT SEED STORAGE PROTEIN REVEALS DETAILS OF AN UNUSUAL SUPERSECONDARY STRUCTURE
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DOI：
10.1073/pnas.88.1.68
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发表时间：
1991-01-01
影响因子：
11.1
通讯作者：
TATHAM, AS
中科院分区：
文献类型：
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作者：
MILES, MJ;CARR, HJ;TATHAM, AS
扫描隧道显微镜已被用来证明基于β -反向旋转的螺旋结构是采用重复序列存在于一组小麦面筋蛋白。这种结构类似于基于弹性蛋白中存在的重复序列合成的多肽形成的β螺旋。小麦面筋和弹性蛋白都具有弹性，可能是螺旋结构促成了这种特性。
Scanning tunnelling microscopy has been used to demonstrate that a spiral structure based on beta-reverse turns is adopted by the repeat sequences present in a group of wheat gluten proteins. This structure is similar to the beta-spiral formed by a synthetic polypentapeptide based on a repeat sequence present in elastin. Wheat gluten and elastin are both elastomeric and it is possible that the spiral structure contributes to this property.