random coil

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

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。

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

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。

Its second structure involved some extended strand and random coil .

二级结构预测发现该蛋白富含延伸链和随机卷曲结构，而且该蛋白还具有极高的亲水性。

Under some conditions , protein will unfold into random coil that loses biochemical function .

在某些情况下，蛋白质将会解折叠成散乱的形状并且失去生物功能。

After kept in air for 30 days , part of the random coil transformed to α helix , but no β sheet structure formed .

空气环境存放30d后，分子构象只会发生无规线团向α螺旋结构的少量转化，而不会向β折叠结构转化。

The structure of regenerated A. pernyi silk fibroin films was the coexistence of α helix and random coil .

指出再生柞蚕丝素膜内丝素蛋白的分子构象为α螺旋和无规线团结构共存。

The transformation from random coil to β - folding of various factors which have influence on the molecular conformations of sericin has also been studied .

并对影响丝胶分子构象从无规卷曲向β&折迭转化的各种因素进行了研究，阐明了易溶丝胶和难溶丝胶的形成和相互转化的机理；

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

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。

CD results suggest that RSF undergoes a conformation transition from random coil to P-sheet . The transition kinetics consists two different rate sections .

圆二色谱的结果表明，再生丝素蛋白发生了由无规线团向β-折叠的构象转变，其动力学经历了两个不同速率的过程。

In the absence of Pb2 + , the thrombin binding aptamer with a random coil structure exhibits a relatively weak scattering intensity .

在没有铅离子存在的情况下，凝血酶适配体以随机的线圈结构存在并且呈现出相对较低的散射强度。

While in far higher concentration of NaOH than transitional concentration , the random coil was the more favorite conformational structures to curdlan molecules ;

在远高于超分子构象转变浓度的溶液中凝聚糖分子成无规线团结构；

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 .

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。

Loss of a-helix gradually transformed into β - sheet and random coil , which the latter two were involved in the structure of the gel . 3 .

丢失的α-螺旋逐步转变成为β-折叠和无规则卷曲，后两者参与了凝胶的结构。

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 .

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。

The two effectors have no signal peptide . The secondary stucture of the two proteins were composed of random coil , alpha helix and extend strand .

二级结构均主要由无规则卷曲、α-螺旋及延伸链组成。信号肽预测显示，两个蛋白均没有信号肽。

Circular dichroism detection indicated the secondary structure of gelatin contains 61.5 % β - turn and 38.5 % random coil without the traditional a-helix and P-sheet .

经圆二色谱检测，明胶的二级结构含有61.5%的β转角和38.5%的无规则卷曲，而不含传统的α螺旋和β折叠。

From the thermal effects , the inactivation of potato PPO in infared radiation is probably caused by a-helix turning to P-turn and random coil .

红外处理下马铃薯PPO失活从热效应方面来看，可能是α-螺旋向β-转角和无规则卷曲转化的转化而造成的。

It was demonstrated that the enzyme has 28.8 % a-helix , 27.9 % p-sheet , 43.2 % random coil by the analysis of circular dichroism spectrum .

圆二色谱（CD）对其二级结构的分析显示，蔗糖酶分子中α-螺旋占28.8%，β-折叠占27.9%，无规则卷曲占43.2%。

In the light of polymer physics , protein folding can be viewed as the process that a special type of polymer chain proceeds from random coil state to compact and ordered globular state .

从高分子科学的角度来看，蛋白质的折叠过程可以理解为一类特殊的高分子从其无规线团状态演变为相对紧致有序的熔球状态的过程。

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 % .

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。

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 .

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 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 .

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。

It was found that with the increase of PGG concentration , the interaction of PGG with HSA has mainly caused the change from the α - helix structure to β - turn and random coil structure .

随着药物浓度的增加，PGG和HSA之间的相互作用主要使HSA的二级结构发生了由α螺旋向β转角和无规结构的转化。

The configuration of the composite was described in terms of the random coil model and scanning electro microscopy ( SEM ) . The effect factors of beating degree , content of basalt fiber and adhesive , etc were discussed .

利用无规线团模型对其结构进行了描述，采用逾渗模型对其过滤性能进行分析，并讨论了打浆度、玄武岩纤维含量、胶粘剂等因素对复合材料性能的影响。

The results showed that without ATP and cDNA , fluorescence intensity of the aptamers was weak , and the majority of the aptamers were closed-loop , and a few of aptamers were random coil .

结果表明，无ATP和cDNA时，核酸适体分子荧光强度较弱，大多数处于闭环状态，少数处于无规则卷曲状态。

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 .

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 showed that the fusion region of BCR-ABL fusion protein ( p210 ~ ( BCR-ABL )) probably lo - cated in a B cell epitope which contained α - helix and random coil structure .

结果表明：BCR-ABL蛋白融合区位于B细胞表位内，该表位含有α-螺旋和无规则卷曲结构。

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 .

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。

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 .

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 through circular dichroism spectrum analysis that the secondary structure of Peak 1 was the most complex , including β - corner ( 31.5 % ), random coil ( 27 % ) and α - helix ( 25.8 % ) .

园二色谱测定酶的二级结构：峰1结构最为复杂，以β-转角为最高，占31.5%，无规线团占27%，α-螺旋占25.8%；