Analysis of Stability on Elastic Plates with Initial Imperfections

ＡＮＡＬＹＳＩＳＯＦＳＴＡＢＩＬＩＴＹＯＮＥＬＡＳＴＩＣＰＬＡＴＥＳＷＩＴＨＩＮＩＴＩＡＬＩＭＰＥＲＦＥＣＴＩＯＮＳＸｕＫａｉｙｕ（徐凯宇）（ＲｅｃｅｉｖｅｄＯｃｔ．５．１９９４；ＣｏｍｍｕｎｉｃａｔｅｄＰａｉＬｉｚｈｏｕ）ＡＮＡＬＹＳＩＳＯＦＳＴＡ...     

脲和盐酸胍诱导的卵清溶菌酶分子去折叠过程中各稳定构象态的分布和过渡

以内源荧光光谱和荧光相图法研究了脲和盐酸胍诱导的卵清溶菌酶分子的去折叠过程,结果表明,当变性液中脲和盐酸胍的浓度分别约为4.0和3.0 mol/L时,卵清溶菌酶分子的去折叠过程均存在一个折叠中间态,这两个去折叠过程均符合"三态模型".在卵清溶菌酶分子"三态"去折叠过程的基础上,通过变性剂分子和卵清溶菌酶分子之间的缔合一...     

Isoentropic and Isoenthalpic Temperatures of Protein Unfolding in Hydrophobic Interaction Chromatography

Hydrophobic interaction chromatography (HIC) is widely used for the separation and purification of biopolymers in their native state, and now also becomes a new method to refold the denatured proteins1. The effect of salt or water concentration2 on the pr…     

Extrinsic fluorescence probe study of human serum albumin using Nile red

Nile red bound to human serum albumin (HSA) shows an order of magnitude increase in the probe's fluorescence intensity. Here, we report on the fluorescence characteristics of the probe-protein complex in Trizma buffer (pH 7.1), urea, guanidine hydrochloride, and AOT/isooctane/buffer reverse micelles using both steady—state and time-resolved fluorescence techniques. With a view to illustrating the use of extrinsic probe fluorescence spectroscopy in protein research, we demonstrate that protein unfolding can be observed through measurements of the probe's time-resolved anisotropy and steady-state fluorescence spectrum. Moreover, this shows that thermal unfolding is fundamentally different from using denaturant, with respect to changes in both the nanosecond diffusional rotation of the probe at intermediate stages and in the denatured protein's structure. Also, the large Stokes shift of Nile red allows the changes in the environment of the probe-protein complex in reverse micelles of varying waterpool size to be easily identified in the steady-state fluorescence. This was not seen in earlier work exploiting the intrinsic tryptophan fluorescence of HSA and further demonstrates the complementary information that extrinsic fluorescence probe studies can offer protein science. We discuss the complex acrylamide quenching characteristics of Nile red bound to HSA in terms of the possibility of at least two binding sites for the probe and the effect of acrylamide on the probe-protein structure at very high quencher concentrations.     

软X光能谱仪求辐射能流的改进方法

使用多道软X光能谱仪测量黑腔辐射能流时间过程并使用最小二乘法将多道谱仪的响应函数线性组合为等效平响应。针对惯性约束聚变实验中软X光能谱强度分布不均匀、等效平响应局部不平带来的误差,提出了辐射能流求解的加权改进算法。对不同谱形和等效积分温度的能谱进行了计算,比较了不同方法得到的能流还原能力。改进后的方法应用于实验数据的处理,得到了修正后的等效积分温度随时间的演化过程。     

Pressure unfolding facilitates the formation of temperature gels

Abstract

The formation of protein aggregates after pressure treatment was investigated by Fourier Transform Infrared Spectroscopy (FTIR). The results show that the pressure unfolded protein ends in a conformation, after the release of the pressure, which has an increased tendency to aggregate, even at temperatures lower than the denaturation temperature of the untreated protein. After pressure pretreatment the infrared spectrum shows the same intermolecular antiparallel β-structure features as observed after a temperature treatment that gives rise to protein gelation. on the other hand, this structure can be destabilized by applying moderate pressures, which are significantly lower than the corresponding denaturation pressure.     

Small angle neutron scattering studies on protein denaturation induced by different methods

Small angle neutron scattering (SANS) has been used to study conformational changes in protein bovine serum albumin (BSA) as induced by varying temperature and in the presence of protein denaturating agents urea and surfactant. BSA has prolate ellipsoidal shape and is found to be stable up to 60°C above which it denaturates and subsequently leads to aggregation. The protein solution exhibits a fractal structure at temperatures above 64°C, with fractal dimension increasing with temperature. BSA protein is found to unfold in the presence of urea at concentrations greater than 4 M and acquires a random coil Gaussian chain conformation. The conformation of the unfolded protein in the presence of surfactant has been determined directly using contrast variation SANS measurements by contrast matching surfactant molecules. The protein acquires a random coil Gaussian conformation on unfolding with its radius of gyration increasing with increase in surfactant concentration      

Chemical Stimulus‐responsive Folding and Unfolding of a Dendrimeric Assembly

A dendrimeric trimer undergoes folding and unfolding in response to a chemical stimulus. The trimer of interest contains a central dendrimer with a butadiyne‐linked zinc porphyrin dimer ((ZnP)₂) core, in addition to two terminal dendrimers with zinc porphyrin (ZnP) cores. The obtained absorption spectra indicate that the unfolded form is the exclusive conformer in chloroform, while the addition of 1,4‐diazabicyclo[2.2.2]octane (DABCO) in chloroform leads to transformation from the unfolded to the folded structure containing two DABCO units per trimer; the folded structure originates from the cross‐linking of (ZnP)₂ and ZnP with DABCO. Moreover, the addition of excess DABCO promotes the generation of the unfolded structure containing four DABCO units.