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MINIMUM FOLDING UNIT OF DYSTROPHIN ROD DOMAIN

机译：失重杆域的最小折叠单元

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摘要

Fragments of the rod domain of dystrophin, which consists of spectrin-like repeating sequences, have been prepared by expression in Escherichia coli. The phasing established earlier for the dystrophin rod, as well as for Drosophila spectrin and smooth muscle alpha-actinin, suggested a length of less than 113 residues for the dystrophin repeat that we have chosen. Fragments with a common N-terminus and lengths between 113 and 119 residues were prepared. The formation of the stable native tertiary fold could be recognized by resistance to proteolysis, the circular dichroism spectrum in the regions of both peptide and aromatic absorption bands and the resolution of the long-wavelength component in the tryptophan absorption spectrum. It was found that the critical length for folding was 117 residues: shortening the chain by 1 further residue resulted in loss of the capacity to form a defined tertiary structure. Residue 117 is a glutamine; replacement of this by a methionine residue did not impair the ability of the chain to enter the folded conformation, implying that it is the length of the C-terminal alpha-helix, rather than any specific side-chain interaction, that is critical in determining the stability of the native structure. The fragment of 119 residues forms a significantly more stable structure than that of 117. It appears that the minimum unit capable of forming the native fold extends some residues into the adjoining sequence repeat.
机译：肌营养不良蛋白的杆结构域的片段，由血影蛋白样重复序列组成，已经通过在大肠杆菌中表达而制备。肌营养不良蛋白棒，果蝇血影蛋白和平滑肌α-肌动蛋白的建立较早，这表明我们选择的肌营养不良蛋白重复序列​​的长度少于113个残基。制备了具有共同N端且长度在113至119个残基之间的片段。稳定的天然三级折叠的形成可以通过对蛋白水解的抗性，在肽和芳族吸收带区域的圆形二向色光谱以及色氨酸吸收光谱中的长波长成分的分辨来识别。发现折叠的临界长度为117个残基：将链再缩短1个残基导致丧失形成确定的三级结构的能力。残基117为谷氨酰胺;用甲硫氨酸残基替代它并不会损害链进入折叠构象的能力，这暗示着C末端α-螺旋的长度而不是任何特定的侧链相互作用对于确定本地结构的稳定性。 119个残基的片段形成了比117个残基更稳定的结构。似乎能够形成天然折叠的最小单元将一些残基延伸到相邻的序列重复序列中。

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