三股螺旋

红外光谱显示PSC保留了大量的三股螺旋结构；

IR spectrum showed that the PSC kept a great amount of triple helix structure .

Coralyne对三股螺旋RNA的识别及稳定作用

RNA Triple-Helix Recognition and Stabilization by Coralyne

十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）谱图，显示了用不同的方法脱脂后所提取的胶原保留了天然的三股螺旋结构，黏度法测得猪皮胶原的变性温度为35.7℃。

And SDS-PAGE electrophoresis analysis shows that the triple helical structure is retained in pigskin collagen , and the denaturation temperature of the collagen measured by viscosity method is 35.7 ℃ .

在DMSO－H2O体系中，体积分数φH2O降至0.2后三股螺旋解离为单股螺旋。

The triple helix abruptly melts into single helix when the φ H2O is decreased to 0.20 ( V / V ) in the H2O-DMSO mixture . The dissociation is reversible .

采用电泳及DSC分析了所得天然胶原的分子质量和变性温度，结果表明：所得天然胶原相对分子质量集中，其变性温度为38.5℃，为保持了三股螺旋结构的天然胶原。

SDS-PAGE electrophoresis and DSC were used to analyze collagen molecular weight distribution and denaturation temperature respectively . Results indicated that the molecular weight was concentrative and the denaturation temperature was 38.5 ℃, showing triple-helix structure of natural collagen .

热变性温度为58.2℃，Zeta电位方法测得其等电点为7.44，园二色谱及红外分析结果显示其保持了胶原的天然三股螺旋构象。

The thermal denaturation temperature of the fiber was 58.2 ℃, and its isoelectric point was 7.44 , which determined by Zeta potential determination method , and its natural triple helix conformation was maintained according to the circular dichroism and FT-IR results .

X-射线衍射显示鸡骨胶原保持完整的三股螺旋结构；

Chicken bone collagen remained tri - helix configuration by X-ray diffraction analysis .

超声波对溶液中胶原蛋白聚集体和三股螺旋结构的影响

Effect of Ultrasonic Irradiation on Aggregate and Triple-helix Structure of Collagen in Acetic Acid Solution

圆二色谱表明，甘油的加入没有改变胶原天然的三股螺旋结构。

The CD spectra showed that the addition of glycerol to the collagen did not damage the native triple helical structure of collagen .

我们的实验表明：在低于超分子构象转变浓度的碱溶液中凝聚糖分子多以三股螺旋的结构存在于溶液中；

Our results showed that in a low concentration of NaOH aqueous solution that was lower than the transitional concentration of helical structure , curdlan mainly maintained its triplex structure ;

圆二色谱分析表明胶原在221nm和192nm处分别有一个特征的正吸收峰和负吸收峰，即典型的胶原三股螺旋结构。

Circular dichroism ( CD ) spectra revealed that there were a positive peak around 221 nm and a negative peak around 192 nm for collagen , which were the characteristics of collagen triple helix .

在胶原的所有提取方法中，酶法是比较理想的提取方法，不仅提取产率高，对环境友好，而且提取的胶原样品基本维持了天然胶原的三股螺旋结构。

The contents and results of this paper are as follows : First , enzyme hydrolysis is the premium extracting method , which has both high productivity , friendly environment and the original triple helix structure .

胶原蛋白α-1（八）链前体（内皮胶原蛋白）至今发现人体胶原蛋白已有19种，带有前肽的三股螺旋胶原分子称为前胶原，水解后成为胶原分子。

Collagen α - 1 ( VIII ) chain precursor ( Endothelial collagen ) has been found 19 species of human collagen , with the former three-helical peptide molecules is called procollagen collagen which can be hydrolyzed to collagen .