无规卷曲

在ATP作用下，无规卷曲状态的核酸适体分子变成闭环状态，荧光强度下降。

In the presence of ATP , aptamers changed into closed loop from random coil , and the fluorescence intensity declined .

mRNA解折叠的链构象与相应新生肽链构象相关性的探索而当湿度小于75%大于40%范围时分子的二级结构改变以β折叠和无规卷曲的肽链构象。

The Correlation Between the Chain conformations of Unfolded mRNA and Corresponding Nascent Polypeptide R 40 % - 75 % , it can be obtained as antiparallel β - cheet and random coil conformation .

预测Ub的3D模型为球型结构，蛋白中有一个α-螺旋和两个反式β-折叠，C端成无规卷曲游离于球型结构之外，与已知泛素结构相似。

The 3D model of ubiquitin was spheroidal , including a a-helix and two β - sheets , and C-terminal was a random coil , which was similar to known ubiquitin structures .

SEB的傅里叶变换红外光谱和激光拉曼光谱分析表明，SEB的二级结构单元主要为β折叠和α螺旋，无规卷曲含量较少，侧链CCSSCC构型为反式扭曲反式。

The secondary structural unit of SEB was mainly composed of P - sheets and a - helixs with few random coils . The side chain conformation of C C S S C C was trans-twist-trans .

而住高浓度CTAB或较长作用时间时，蛋白质的二级结构被破坏，蛋白质内部氧键减弱，部分的α-螺旋结构转变为无规卷曲结构。

During long interaction period or at high concentration of CTAB , CTAB unfolded the protein by decreasing the α - helix structure and increasing the random coil .

测定茧丝中的内、中、外层丝胶的CD谱表明，从外层到内层有由无规卷曲结构转变为β折叠结构的趋势；

As for the inner , middle and outer layers of sericin in a bave , the tendency for conversion from random-coil to β - folded structures , from inner to outer layers , has been shown by the circularly dichromatic measurement .

应用圆二色仪初步测定了重组蛋白的二级结构，重组SD的二级结构中大约有29.2%的α螺旋，9.3%β折叠，32.7%β转角，28.8%无规卷曲。

Circular dichroism studies on the recombinant SD indicated that the secondary structure of the recombinant protein had about 29.2 % α - Helix , 9.3 % β - Sheet , 32.7 % β - Turn , 28.8 % Random coil .

圆二色谱（CD）分析了鹰嘴豆分离蛋白的二级结构：α-螺旋36.2%，β-折叠28.4%，转角10.3%，无规卷曲25.2%。

The secondary structure analyzed by circular dichroism ( CD ) showed that , α - helix , β - sheet , turn and random coil were 36 . 2 % , 28 . 4 % , 10 . 3 % and 25 . 2 % , respectively .

圆二色性测定发现热处理后蛋清形成了以β-折叠和无规卷曲为主的二级结构，蛋清经热处理引起的蛋白质的二级结构变化对DH的影响不大。

Circular dichroism measurement found the formation of a β - sheet and random coil-based secondary structure in egg white proteins after heat treatment . The structural changes caused by the heat treatment of egg white proteins contributed little to the DH growth .

而明胶和胶原水解物的正吸收峰消失，表现为典型的无规卷曲构象。

However , gelatin and collagen hydrolysate did not have positive peaks around 220 nm , suggesting random coils .

根据谱图变化可以看出，随着温度的降低，部分β－折叠和无规卷曲结构将转变为有序的α－螺旋结构。

The transition of β - and disordered structure to α - helix structure is found as temperature decreased .

这两个位点分别处于结构域1的1个β-折叠片和一段无规卷曲上，参与和T2/T3三核簇的连接。

They both located in Domain 1 , which participated in connection of T2 / T3 trinuclear cluster . 2 .

二级结构预测，显示该蛋白主要以a-螺旋和无规卷曲为主，含少量的β-折叠，间或有B-转角。

Secondary structurs of the protein were mainly alpha helixes and random coils , and little beta sheet and beta turn .

经金属盐和氧化剂还原剂处理的彩丝内部有部分β-折叠构象转变成了无规卷曲。

There are some β - sheet changed into random coil after treated by metal salt , oxidants and reducing agent .

在肌球蛋白凝胶形成过程中，肌球蛋白分子充分伸展、转变为有利于肌球蛋白重链交联的无规卷曲结构。

During the forming of myosin gel , myosin molecules extended and changed into random coil contributed to myosin heavy chain cross-linking .

在溶液中的构象是α-螺旋10.6%，β折叠16.3%和无规卷曲73.1%。

Its dispersion of secondary structure in solution showed 10.6 % α - helix , 16.3 % β - form and 73.1 % unordered .

表明蓖麻蚕茧丝的丝素分子构象中除了有无规卷曲结构和β折叠结构外，还存在着α螺旋结构。

The results show that the molecules are arranged in random coiling and β chain folding structures , as well as in α helical conformation .

由此可知，随着加热温度的升高和加热时间的延长，其α-螺旋、B-折叠含量逐渐减少，β-转角含量呈升高趋势，而无规卷曲含量逐渐增加显著。

Therefore , the content of a-helix , B-sheet gradually reduced , while B-turn and the random coil increased as increasing heating temperature and heating time .

丝胶二级结构主要以无规卷曲结构为主和部分β构象，含有74.61%的极性侧链氨基酸。

Sericin consists of random coil and β structure , in which the former is the main part . The content of amino acids which have polar side chains is as high as 74.61 % .

研究发现，电化学还原过程诱导微过氧化物酶-11的构象由无规卷曲向α螺旋转变，这为进一步理解生物电子传递过程与生物分子构象转变机理提供了基础信息。

The results showed that the electrochemical reduction induced the conformational transition of MP-11 from random coil to α - helix and provided an important information for understanding biological electron transfer mechanism coupled with conformational transitions .

茧丝的外层丝胶溶液的构象由无规卷曲向β折叠结构转变是一个自发过程，而茧丝蜡的存在能加速这一转变过程。

The conformational conversion of the sericin solution of the outer layer of the bave from random-coil to β - folded structure is a spontaneous process which can be accelerated in the presence of waxy substance .

空间结构模拟表明，该蛋白的内部主要是β-折叠和一些无规卷曲，可能是酶与底物结合的活性中心，外围主要是α-螺旋。

Spatial structure simulation indicated that periphery of this protein was α - helix , and inside were P-pleated sheet structure and random coil , perhaps it was the active centre of the combination of this protein and its substrate .

结果表明：在1.0~6.0kV.cm-1范围，不同强度的电场对辣根过氧化物酶的α-螺旋、β-折叠、β-转角及无规卷曲相对含量的影响程度不同。

The results show that different electric field strength ranging from 1.0 to 6.0 kV · cm-1 has a different effect on the relative contents of α - helix ,β - sheet ,β - turn and random coil of the HRP .

发现再生丝素水溶液在静置存放过程中会有结构的变化即无规卷曲和α螺旋向β折叠结构的转变，并且浓度越大，构象转变越快。

It was found that the conformation of silk fibroin was changed from random coil and α - helix to β - sheet structure during the storage . And the higher the solution concentration is , the more the conformational transformation .

此时的最大发射峰为338nm，圆二色光谱分析二级结构表明α-螺旋占27.24%，β-折叠占24.48%，无规卷曲为48.28%，呈典型球蛋白特征。

Circular dichroism ( CD ) spectrum analysis showed that the percentage of α - helix ,β - sheet and random coil of day lily tubulin is 27.24 % , 24.48 % and 48.28 % , respectively , indicating a typical feature of globulin .

由圆二色光谱可知，丝素结构从液态时的无规卷曲转化为凝胶态时的β构象，其干胶粉末经红外吸收光谱证实为β构象。

Based on the CD spectra , it was found that the structure of fibroin was changed from random coil to β - conformation during gelation . And the structure of dried gel powder was confirmed to be β - conformation according to the IR spectra .

随着压力的增加，无规卷曲含量逐渐增加，二硫键构象变化使得蛋白稳定性降低，酪氨酸残基包埋于侧链中，紧密折叠结构得以舒展。

Along with the increase of pressure , the content of random coil was increasing gradually , the stability decreasing owing to the conformation change of disulfide bonds , and tyrosine was buried in the side chain , accordingly the compactly plate sheet structure was to become loose .