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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Secondary structures at polypeptide-chain termini and their features.
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Secondary structures at polypeptide-chain termini and their features.

机译：二级结构在多肽链末端和他们的特性。

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摘要

An analysis of secondary structures (alpha-helices and beta-strands) in the two terminal regions of polypeptide chains reveals features different from those observed over the whole protein structure. Compared with the overall distribution, the helices in the N-terminal region tend to be smaller and have higher propensities to contain Gln and Leu, while the C-terminal helices are longer and have a greater proportion of Lys and Glu. As a strand, the C-terminal region is never found in the interior of parallel beta-sheets and has a higher propensity to be at the edge of antiparallel beta-sheets. In contrast, compared with the whole structure the N-terminal region has a higher propensity to be in the interior of parallel beta-sheets. Compared with the overall distributions, terminal helices and strands show distinct periodicities in length. The Schellman motif, which is a prevalent C-capping motif in helices, is not common in C-terminal helices. There are other observations that can be used in the design of helical peptides: more residues beyond the C-terminus of helices are used for capping interactions than residues before the N-terminus. Consideration of the distribution of terminal strands in the interior and at the edge of beta-sheets suggests a sequential folding mechanism beginning at the N-terminus of the polypeptide chain.
机译：二级结构的分析(阿尔法螺旋和beta-strands)的两个终端区域多肽链显示特性不同从这些观察到在整个蛋白质结构。分布、氨基的螺旋线地区往往是越来越高倾向包含Gln和低浓缩铀,而c端螺旋更长和更大赖氨酸和Glu的比例。c端地区在室内中是找不到的平行的β折叠和更高倾向反平行的边缘β折叠。结构的n端地区更高倾向于在内部的并行β折叠。分布,终端螺旋线和链不同周期的研究。主题,这是一个普遍C-capping主题在c端螺旋螺旋线,并不常见。还有其他可以用于观察设计的螺旋肽:更多的残留超出了螺旋线的糖基用于比之前残留限制交互n端。终端链在内部和边缘的β折叠显示顺序折叠机制的n端开始多肽链。

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