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    The effects of guanidine hydrochloride on the 'random coil' conformations and NMR chemical shifts of the peptide series GGXGG.
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    The reversible denaturation of protein disulfide isomerase proceeds through intermediates that are stabilized by interaction with guanidine hydrochloride. At pH 7.5, the equilibrium denaturation by urea is completely reversible and the transition can be reasonably well-described by a two-state model involving only native and denatured forms. In comparison, the equilibrium denaturation by guanidine hydrochloride occurs in two distinct steps. In the presence of a low constant amount of guanidine hydrochloride (0.5-1.4 M), urea denaturation also becomes biphasic, suggesting the accumulation of an intermediate species that is stabilized by specific interaction with guanidine hydrochloride but not by high concentrations of other salts or other denaturants.
    Guanidine
    Denaturation (fissile materials)
    Hydrochloride
    Equilibrium unfolding
    Citations (73)
    展开脲和 guanidine hydrochloride 导致的牛的心细胞色素 c 通过他们的内在的荧光排放系列,荧光阶段图,熄灭的荧光,尺寸排除层析,本国的 polyacrylamide 胶化 electrophoreses 和释放侧面被学习。结果证明在他们在脲和 guanidine hydrochloride 答案展开期间,牛的心细胞色素 c 分子仅仅在一种 unimolecular 形式和他们的双分子或多分子的总数和总数存在猛抛没始终被形成。在变性作用答案的脲和 guanidine hydrochloride 集中是什么时候独立大约 6.0 和 3.0 mol/L,他们能完全被撤销,色氨酸,残余原来在他们的分子的内部嵌入的几乎所有暴露于他们的分子的表面。与展开最经常使用的马心细胞色素 c 不同,脲和 guanidine hydrochloride 导致的牛的心细胞色素 c 的是独立一个完全合作的过程并且跟随了一个二状态的模型。
    Guanidine
    Hydrochloride
    Citations (0)
    Abstract By analyzing the effect of urea and guanidine hydrochloride on the circular dichroism of many polypeptides and proteins, it is concluded that under conditions of high concentration of the perturbant and at low temperatures the resultant state approached is that of a local extended helix structure instead of a completely random coil. Intensification by urea and guanidine hydrochloride of the circular dichroism bands of poly‐ L ‐proline II leads to the proof that the mechanism of interaction of urea and guanidine hydrochloride with proteins is through hydrogen bonding to the backbone carbonyl group.
    Guanidine
    Hydrochloride
    Random coil
    Denaturation (fissile materials)
    Citations (130)
    四综合了包括 polyhexamethylene guanidine hydrochloride 和它的三新类似物,有不同烷基链长度的 biocidal guanidine hydrochloride 聚合物被用来与 phospholipids 泡 mimicking 调查他们的相互作用细菌的膜。描述被使用荧光染料漏,等温的滴定热量测定,和微分扫描热量测定进行。结果证明聚合物的逐渐地变长的烷基链增加了 biocidal 活动,与增加的染料漏率和增加的有约束力的常数和 polymermembrane 的精力变化价值伴随了相互作用。polymermembrane 相互作用导致了 pretransition 的变化和 phospholipids 泡的主要阶段转变(减少的温度和增加的宽度) ,建议在 phospholipids headgroups 的 conformational 变化和在类脂化合物膜的恐水病的区域的 disordering。上述信息表明 guanidine hydrochloride 聚合物的膜混乱行动是聚合物到 phospholipids 膜和极的 headgroups 和 phospholipids 膜的恐水病的核心区域的随后的不安的强壮的绑定的结果。烷基链结构显著地影响有约束力的常数和 polymermembrane 相互作用和 phospholipids 膜的不安程度的精力变化价值,它导致聚合物类似物的不同 biocidal 活动。这个工作关于 biocidal guanidine hydrochloride 聚合物的膜混乱行动机制提供重要信息。
    Guanidine
    Hydrochloride
    Citations (0)
    The denaturation of lysozyme by guanidine hydrochloride and hydrochloric acid, and by guanidine hydrochloride alone at 25 °C was studied using a dilatometric technique. From results of the dilatometric measurements volume changes for partial and complete denaturation by hydrochloric acid at constant guanidine hydrochloride concentration were determined. The volume change due to unfolding per se in 3 M guanidine hydrochloride was found to be — 47 ml per mol of lysozyme. Volume changes were also determined for partial and complete denaturation of lysoyzme at 25 °C by guanidine hydrochloride alone at constant pH. The volume change due to unfolding per se in 6 M guanidine hydrochloride and pH 5.2 was determined to be — 54 ml per mol of lysozyme.
    Guanidine
    Hydrochloride
    Hydrochloric acid
    Denaturation (fissile materials)
    The GST-PR-1a was induced by optimized conditions,and fluorescence spectra were used as the probe to investigate the thermal stability,urea and guanidine hydrochloride degeneration of purified recombinant GST-PR-1a proteins. The fluorescence intensity of PR-1a was reduced slightly when treated at 50 ~ 80 ℃. However,it was strongly weakened at 90 ℃. With the urea and guanidine hydrochloride treatment,the maximum absorption wavelength occurs red shift along with the increase of the concentration. The results indicate that tryptophan residues are mostly in the interior of PR-1a protein. Factors such as temperature can change its 3D-structure.After specific concentrations of guanidine hydrochloride treatment,protein presents intermediate state.
    Guanidine
    Hydrochloride
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