CONFORMATIONAL INTERMEDIATES IN THE FOLDING OF A COILED-COIL MODEL PEPTIDE OF THE N-TERMINUS OF TROPOMYOSIN AND ALPHA-ALPHA-TROPOMYOSIN
CONFORMATIONAL INTERMEDIATES IN THE FOLDING OF A COILED-COIL MODEL PEPTIDE OF THE N-TERMINUS OF TROPOMYOSIN AND ALPHA-ALPHA-TROPOMYOSIN
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DOI：
10.1002/pro.5560020809
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发表时间：
1993-08-01
期刊：
影响因子：
8
通讯作者：
HITCHCOCKDEGREGORI, SE
中科院分区：
文献类型：
--
作者：
GREENFIELD, NJ;HITCHCOCKDEGREGORI, SE
圆二色性被用来研究α-原肌球蛋白和AcTM 43的折叠，AcTM 43是一种43个残基的肽，被设计成作为原肌球蛋白N-末端结构域的模型。肽的序列为AcMDAIKKKMQMLKLDVENLLDRLEQLEADLKALEDRYKQLEGGC。该肽在低温下似乎形成卷曲螺旋（
Circular dichroism was used to study the folding of alphaalpha-tropomyosin and AcTM43, a 43-residue peptide designed to serve as a model for the N-terminal domain of tropomyosin. The sequence of the peptide is AcMDAIKKKMQMLKLDVENLLDRLEQLEADLKALEDRYKQLEGGC. The peptide appeared to form a coiled coil at low temperatures (