Tskhovrebova L, Trinick J
Division of Molecular and Cell Biology, Veterinary School, Bristol University, Langford, UK.
J Mol Biol. 1997 Jan 17;265(2):100-6. doi: 10.1006/jmbi.1996.0717.
"Molecular combing" induced by a receding meniscus has been shown to extend individual titin molecules. Electron microscopy reveals that both ends of the molecule tend to attach to a mica substrate, probably due to their local positive charges. This leaves the remainder of the molecule free to be straightened and extended by forces of up to approximately 800 pN. A small region in the I-band part of the molecule, which probably corresponds to sequence high in P, E, V and K residues, is the most compliant and appears to extend by an unfolding of the polypeptide chain. Other parts of the molecule are also capable of extension. These mechanical extensions in titin are probably reversible.
由后退弯月面诱导的“分子梳理”已被证明可伸展单个肌联蛋白分子。电子显微镜显示，该分子的两端往往会附着在云母基质上，这可能是由于其局部正电荷所致。这使得分子的其余部分能够在高达约800皮牛的力的作用下自由伸直和伸展。分子I带部分的一个小区域，可能对应于富含脯氨酸、谷氨酸、缬氨酸和赖氨酸残基的序列，是最具柔韧性的，并且似乎通过多肽链的展开而伸展。分子的其他部分也能够伸展。肌联蛋白中的这些机械伸展可能是可逆的。
