The pressure tolerance of different poly-l-lysine conformers in aqueous solution: Infrared spectroscopy and two-dimensional correlation analysis

Poly-l-lysine can form either of three different conformers as α-helix, anti-parallel β-sheet and random coil stably under appropriate conditions. In buffer solution poly-l-lysine exists in a random coil at about pH 4, an α-helix above pH 12, and transforms from α-helix to β-sheet when the sample is heated to 46 °C for 30 min. The effects of elevated hydrostatic pressure on three different initial conformers of poly-l-lysine are investigated with Fourier transform infrared spectroscopy and two-dimensional correlation analysis. Changes observed in the amide I′ band indicate that the α-helix conformer undergo hydration enhancement at low pressure (<400 MPa), then gradually transition into an α′-helix. Two initial conformers, the β-sheet and random coiled polypeptide, undergo conformational changes to an α-helix at low pressure and to an α′-helix at high pressure. Moreover, the conversion occurred at a lower pressure for the β-sheet (∼250 MPa) than for the α-helix (∼300 MPa) and the random coil (∼850 MPa).     

Raman光谱研究铜锌超氧化物歧化酶及其金属取代衍生物的二级结构

本文测定了铜锌超氧化物歧化酶（Cu2Zn2SOD)及其金属取代衍生物Cu2Ni2SOD的Raman光谱,对图谱进行了归属,并定量测定了两种SOD的二级结构,同时对结构与活性的关系进行了讨论。     

The studies of FT-IR and CD spectroscopy on catechol oxidase I from tobacco

A novel copper-containing enzyme named COI (catechol oxidase I) has been isolated and purified from tobacco by extracting acetone-emerged powder with phosphate buffer, centrifugation at low temperature, ammonium sulfate fractional precipitation, and column chromatography on DEAE-sephadex (A-50), sephadex (G-75), and DEAE-celluse (DE-52). PAGE, SDS-PAGE were used to detect the enzyme purity, and to determine its molecular weight. Then the secondary structures of COI at different pH, different temperatures and different concentrations of guanidine hydrochloride (GdnHCl) were studied by the FT-IR, Fourier self-deconvolution spectra, and circular dichroism (CD). At pH 2.0, the contents of both alpha-helix and anti-parallel beta-sheet decrease, and that of random coil increases, while beta-turn is unchanged compared with the neutral condition (pH 7.0). At pH 11.0, the results indicate that the contents of alpha-helix, anti-parallel beta-sheet and beta-turn decrease, while random coil structure increases. According to the CD measurements, the relative average fractions of alpha-helix, anti-parallel beta-sheet, beta-turn/parallel beta-sheet, aromatic residues and disulfide bond, and random coil/gamma-turn are 41.7%, 16.7%, 23.5%, 11.3%, and 6.8% at pH 7.0, respectively, while 7.2%, 7.7%, 15.2%, 10.7%, 59.2% at pH 2.0, and 20.6%, 9.5%, 15.2%, 10.5%, 44.2% at pH 11.0. Both alpha-helix and random coil decrease with temperature increasing, and anti-parallel beta-sheet increases at the same time. After incubated in 6 mol/L guanidine hydrochloride for 30 min, the fraction of alpha-helix almost disappears (only 1.1% left), while random coil/gamma-turn increases to 81.8%, which coincides well with the results obtained through enzymatic activity experiment.     

硫酸铜诱导烟草多酚氧化酶抗变性的研究

In order to investigate the interaction between exogenous Cu2+ and Polyphenoloxidase (PPO) from Nictiana Tobacum, the Cu2+-induced resistant-denaturation against guanidine hydrochloride(Gdn-HCl) was studied by the following enzymatic activity assay, fluorescence spectroscopy and circular dichroism (CD). The results show that the GdnHCl-induced unfolding is a two-state process with no detectable inter mediate state in the absence of exogenous Cu2+, while the GdnHCl-induced unfolding in the presence of 10.0 mmol/L exogenous Cu2+ follows a three-state transition with an intermediate state, which results from the fact that Cu2+ increases the structural stability of native PPO and its intermediate. In terms of enzymatic activities, 6 mol/L GdnHCl makes PPO lose 81.4% of its original activity after 5 min, inactivate completely after 30 min, while in the presence of 10.0 mmol/L exogenous Cu2+, only 39.4% and 75.1%, after 5 and 30 min respectively. According to the CD measurements, the relative average fractions of α-helix, anti-parallel2-sheet, 2-turn/parallel 2-sheet, aromatic residues and disulfide bond, and random coil/γ-turn are 1.1%, 3.8%, 3.3%, 7.5% and 84.3%, respectively, in the 6.0mol/L GdnHCl containing no CuSO4, but34.2%, 13.7%, 21.0%, 9.5% and 21.6%, respectively, in the same concentration of Gdn-HCl containing 10mmol/L CuSO4.     

Crystal Structure of Crotin Ⅱ at 2.5  Resolution

1INTRODUCTIONTheplanttoxin,CrotinIisoneoftheribosomeinactivatingproteins(RIPs)[l3.AccordingtothemolecularmechanismofactiontheRIPscanbedividedintotwokinds[2:.OnebelongstoRNAN-glycosidasewhichisclassifiedastwotypes.TypeIconsistsofasinglepolypeptidechain,forexample,trichosanthinandsaporin-Typellconsistsoftwochains,suchasricinandabrin'ThiskindofRIPshydrolysesasingleN-glycosidicbondbetweenanadenineandriboseatspecificnu-cleotide(A4324)of28SrRNAintheribosomes[3i.ThesecondkindofRIPsbel…     

Spectral Study on the Interactions Among Cu(Ⅱ), Doxorubicin and CopC

Interactions among Cu(Ⅱ),doxorubicin and copper operon C(CopC)have been investigated in detail by means of fluorescence,UV-Vis,IR spectra,isothermal titration calorimetry(ITC)and molecular docking in Tris-HCl buffer(50 mmol/L,pH=7.4,25℃).The results suggest that Cu(Ⅱ)-doxorubicin is formed in a Cu(Ⅱ)to doxorubicin molar ratio of 1:2,and the conditional stability constant,K[Cu(Ⅱ)-doxorubicin]is 1.90×10^9 L^2/mol^2,CopC and doxorubicin can form a 1:1 complex,the conditional stability constant is greater than 10^5 L/mol.Binding of doxorabicin causes a conformational change in CopC with the reduction of β-sheet and increase of random coil,and the stability of CopC is decreased.Cu(Ⅱ),doxorubicin and CopC can form a CopC-Cu(Ⅱ)-doxorubicin ternary complex.The formation of CopC-Cu(Ⅱ)-doxorubicin reduced greatly the reduction rate of Cu(Ⅱ)by ascorbate(Vc),i.e.,the binding of doxorubicin affects the action of CopC as redox switch.     

在多孔有机聚合物中构筑广谱性重金属离子吸附活性位

以三维刚性结构的三蝶烯为单体, 通过简单的Friedel-Crafts烷基化反应制备得到高比表面积的三蝶烯基多孔有机聚合物(TPOP), 在TPOP中接枝乙二胺和氯乙酸钠, 构建了广谱重金属离子吸附剂(TPOP-CH₂EDTA). 获得的TPOP-CH₂EDTA具有微孔/介孔结构, 其微孔尺寸为1.6 nm, BET比表面积为634 m²/g, 利于重金属离子传递和配位作用的强化. TPOP-CH₂EDTA对重金属离子具有吸附广谱性, 其对Ag(Ⅰ), Cu(Ⅱ), Ni(Ⅱ), Zn(Ⅱ), Co(Ⅱ), Sn(Ⅳ), Pb(Ⅱ), Cd(Ⅱ), Fe(Ⅲ)和Cr(Ⅲ)等10种重金属离子的去除率均高于98%. 以Pb(Ⅱ)为典型的重金属污染物, 通过Langmuir模型计算得到Pb(Ⅱ)的最大吸附容量高达184.5 mg/g; 具有拟二级吸附动力学特征, 吸附速率快, 动力学常数k₂为0.0173 g·mg^?1·min^?1; 经过5次循环使用后, Pb(Ⅱ)的去除效率仍高达95.8%. TPOP-CH₂EDTA对混合溶液中Pb(Ⅱ)和Cu(Ⅱ)的去除率均高于99%, 且对含有大量无机盐[如Ca(Ⅱ), Mg(Ⅱ), K(Ⅰ)和Na(Ⅰ)离子]和有机化合物的复杂真实水体系, Pb(Ⅱ)和Cu(Ⅱ)的去除效率仍高于90%. 因此, 通过调控多孔有机聚合物微观结构(如比表面积、 孔径和吸附位点密度)而构筑的广谱性重金属吸附材料, 为协同去除复杂水系统中混合重金属离子提供了方案.     

布南色林与人血清白蛋白相互作用的光谱学研究

采用荧光光谱研究了模拟生理务件下抗精神病药布南色林与人血清白蛋白的相互作用,结果表明,布南色林对人血清白蛋白的内源性荧光具有猝灭作用且猝灭方式为静态猝灭.布南色林与人血清白蛋白形成了1∶1的复合物,结合常数K=1.80×104L/mol,且金属离子对结合反应具有较显著的影响.根据不同温度下的热力学函数确定了布南色林与人...     

丝素褐藻糖胶共混膜的结构与热性能

丝素是蚕丝的主要成分，是人类最早应用的天然蛋白质之一，作为性能优良的天然纤维一直用于纺织行业．近年来，丝素膜由于具有良好的透气透氧性和较少的炎症反应，尤其是对活体组织具有良好的生物相容性的特点，在生物工程和生物医学领域得到广泛地研究，被用作酶的固定化材料和哺乳动物细胞培养的基质、体外组织工程支架和抗凝血材料等．     

丝胶蛋白质与铜(Ⅱ)的配位反应

本文运用pH滴定、光谱法、电子自旋波谱、X射线衍射研究丝胶蛋白质与铜 (Ⅱ )的配位反应及其络合物的高次结构 .当溶液的 pH >9 1时 ,丝胶蛋白质与Cu(Ⅱ )生成了稳定的络合物 ,此络合物具有拉伸八面体Cu(N) 4(OH-) 2 型配位结构 ,高次结构为无规卷曲非晶结构 .