Interruption of a 3(10)-helix by a single Gly residue in a poly-Aib motif: a crystallographic study.

Interruption of a 3(10)-helix by a single Gly residue in a poly-Aib motif: a crystallographic study.
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聚 Aib 基序中单个甘氨酸残基对 3(10) 螺旋的中断:晶体学研究。

DOI:
10.1002/bip.21535
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发表时间:
2011
期刊:
影响因子:
2.9
通讯作者:
Solà J
Solà J
中科院分区:
生物学4区
文献类型:
--
作者:
Solà J

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用X射线晶体学方法研究了单个Gly残基插入aib16同聚物对其结构的影响。发现肽N3Aib8GlyAib8PheNH2(1)和CbzPheAib8GlyAib8(2)采用明确的螺旋结构,其大致为310螺旋结构。事实上,2是迄今为止报道的最长的310螺旋晶体结构。然而,在中心Gly残基区域,两种多肽的310结构都出现松动,清楚地表明残基7-9区域局部采用α‐螺旋结构。©2010 Wiley期刊公司生物工程学报(英文版),2011。
The structural influence of a single Gly residue inserted into an Aib16homooligomer was studied in the solid state by X‐ray crystallography. The peptides N3Aib8GlyAib8PheNH2(1) and CbzPheAib8GlyAib8(2) were found to adopt well‐defined helical structures, which are broadly 310helical. Indeed,2is the longest crystallographic 310helix thus far reported. However, in the region of the central Gly residue, a loosening of the 310structure is observed in both peptides, with1clearly showing local adoption of an α‐helical structure in the region of residues 7–9. © 2010 Wiley Periodicals, Inc. Biopolymers 95: 62–69, 2011.
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