胃肠道正常组织与相应肿瘤组织结构的FTIR光谱研究

本文用傅里叶变换红外显微光谱对一系列胃肠道（食道、胃、结肠）肿瘤组织和相应正常组织的冰冻切片进行了研究。结果显示，所有肿瘤组织的光谱基本一致。而正常组织的光谱按１４００－９５０ｃｍ＾－１区域的特点可分为三类。对光谱中蛋白质酰胺Ｉ带曲线拟合的结果表明，正常组织和肿瘤组织中蛋白质的二级结构有着很大的差别。     

H2O／KDEHP（75%）—HDEHP（25%）／n—HEPTANE微乳体系表面活性剂？…

利用傅里叶变换拉曼光谱和傅里叶变换红外光谱对Ｈ２Ｏ／ＫＤＥＧＰ（７５％）－ＨＤＥＨＰ（２５％）／ｎ＝ＨＥＰ－ＴＡＮＥ微乳体系的表面活性剂疏水链和极性头基与水分子的相互作用进行了研究。结果表明：当加水量由Ｗ０＝１增加至４３时,表面活性有性头基［ＰＯ２］＾－的反对称伸缩振动由１２３３ｃｍ＾－１移至１２０７ｃｍ＾－１,其对称伸缩振动由１０９４ｃｍ＾－１移至１０８９ｃｍ＾－１。表面活性剂疏水链的堆结构也发     

DNA构象研究中脱氧核糖拉曼信号的作用

小牛胸腺ＤＮＡ水溶液激光拉曼谱中，表征鸟嘌呤核苷糖环折叠分别为Ｃ３’内式与Ｃ２’内式的特征模６７１与６８２ｃｍ＾－１同时存在，我们认为这表明在ＤＮＡ水溶液中具有Ａ－ＤＮＡ与Ｂ－ＤＮＡ两种构象。计算出６７１ｃｍ＾－１相对含量为３９．４％，与用我们提出的Ｂｒｏｗｎ改进法Ｉ８０７／Ｉ１１００计算得出的３５％Ａ型ＤＮＡ构象含量相接近。其它的脱氧核糖构象拉曼模与磷酸脱氧核糖骨架振动特征模也定性地表明了同样的     

新间接紫外光度法测定微量SO3^2—

在ｐＨ７．０混合磷酸盐介质中,ＳＯ３＾２－使Ｉ３＾－与ＣＴＭＡＢ生成离子缔合物ＣＴＭＡ＾＋,Ｉ３＾－而褪色,从而建立了测定ＳＯ３＾２－的新间接紫外光度法,测定波长为３６５ｎｍ,ＳＯ３＾２－浓度在０－２５μｇ／２５ｍＬ内服从比耳定律,表观摩耳吸光系数为ε＝６．０４×１０＾４Ｌ·ｍｏｌ＾－１·ｃｍ＾－１,可用于食品中微量ＳＯ３＾２－的测定,其结果满意。     

香兰素对甲苯胺希夫碱稀土配合物的红外光声光谱

研究了香兰素对甲苯胺希夫碱及其金属配合物在３８００－２００ ｃｍ＾－１范围的傅里叶变换红外光谱光谱，对主要谱带进行了经验归属。     

高增透的类金刚石碳膜的红外吸收特性研究

利用射频等离子体分解甲烷的技术在锗片上沉积了非晶结构的类金刚石碳膜,傅里叶红外光谱仪测量显示镀覆的类金刚石碳膜的锗片在红外范围内具有高增透作用,特别在１７４０～！２０４４ｃｍ＾－１其峰值透过率高达９９％,在９４５．７ｃｍ＾－１（１０．６ｕｍ）处透过率为９４．５％。利用实测的液内的吸收系数接近于０,在１０．６ｕｍ的吸收系数为２３０ｃｍ＾－１,膜主要由ｓｐ＾３的Ｃ＿Ｈ键结构组成,各吸收峰均得到了很好的     

对Bi-2212超导体中的Raman谱指认

本文对Ｂｉ２－ｘＰｂｘＳｒ２ＣａＣｕ２Ｑδ（ｘ＝０￣０．５）系列样吕以及在真空下不同温度退火的Ｂｉ１．６Ｐｂ０．４Ｓｒ２ＣａＣＵ２Ｏδ样品进行了Ｘ射线衍射和Ｒａｍａｎ谱实验研究。测量表明,随着退火温度的升高,ａ,ｂ,ｃ轴晶格常数增加,与Ｏ（１）ＣｕＢｇ模式相关的２９４ｃｍ＾－１的峰强减少,峰位红移。研究结果进一步表明,４６４ｃｍ＾－１和６３０ｃｍ＾－１峰分别与Ｏ（３）ＢｉＡ１ｇ和Ｏ（２）ＳｒＡ１ｇ     

LaH2分子基态（C2V,A1）的势能函数

在ＱＣＩＳＤ水平上基于相对论紧致有效势（ＲＣＥＰ：Ｒｅｌａｔｉｖｉｓｔｉｃ Ｃｏｍｐａｃｔ Ｅｆｆｅｃｔｉｖｅ Ｐｏｔｅｎ－ｔｉａｌ）方法优化出ＬａＨ２分子的基态为Ｃ２ｖ（Ｘ＾２Ａ１）构型,其〈ＨＬａＨ－１２４４°、平衡核间距Ｒｅ＝２．１９４５Ａ和离子解能Ｄｅ＝５．５９９ｅＶ,并计算出谐振频率：ｖ１＝１２１６．５２１ｃｍ＾－１、ｖ２＝１０８７．４１７ｃｍ＾－１和ｖ３＝２１５６．９５７２ｃｍ＾－１。     

人乳腺癌组织的特征红外光谱研究

应用傅里叶变换红外光谱对２０例人乳腺病理样品进行了分析。实验发现,乳腺癌组织与乳腺良性病变组织之间有较大的红外光谱差异。与乳腺良性病变组织比较,乳腺癌组织的红外光谱中磷酸二酯基团反对称伸缩振动向短波方向位移了２ｃｍ＾－１,其对称伸缩振动向短波方向位移了３ｃｍ＾－１,Ｃ－Ｏ伸缩振动吸收Ａ１１７３／Ａ１１６３比值增加,Ａ１０２５／Ａ１０８２比值下降;ＣＨ３的反对称及对称伸缩振动减弱,ＣＨ２的对称及反对     

Tl—1223超导体及其复Ag带的制备

研究了用产中分熔化法制备Ｔｌ－１２２３超导体的工艺。样品的名义组成为（Ｔｌ０．５Ｐｂ０．５）（Ｓｒ０．８Ｂａ０．２）Ｃａ２Ｃｕ３Ｏｙ。经熔化退火的样品，其磁化电流的７７Ｋ和１Ｔ下大于２×１０＾４／ｃｍ＾２。用熔化－退火的超导粉作原料制得的复Ａｇ带短样，Ｊｃ达１．６－１．７×１０＾４Ａ／ｃｍ＾２（７７ｋ，０Ｔ）。采用烧结后的超导粉作原料，在制备复Ａｇ带的工艺中，如用熔化－退火的热处理制度，可以免除…     

The effect of disulfide bonds on protein folding,unfolding, and misfolding investigated by FT–Raman spectroscopy

Disulfide bond is relevant to many protein folding/unfolding functions and conformational diseases. To elucidate the effects of disulfide bonds on protein folding, unfolding, and misfolding, we performed Fourier transform–Raman measurements on serial chemical‐induced denaturations of bovine serum albumin (BSA). By directly monitoring Raman stretching at S–S (~507 cm⁻¹), S–H (~2566 cm⁻¹), amide I (1655 cm⁻¹ for α‐helix; 1667 cm⁻¹ for β‐sheet structure), and amide III (>1300 cm⁻¹ for α‐helix; 1246 cm⁻¹ for β‐sheet structure), the status of disulfide bonds and secondary structure of BSA at different states were elucidated. Both disulfide bonds and secondary structure (mostly in α‐helix) of BSA appeared relatively stable even when the protein was unfolded by urea solution. However, disulfide bonds were completely reduced and protein secondary structure changed from α‐helix to a relatively β‐sheet dominant when the protein was modified by the mixed solution of urea and dithiothreitol (urea/DTT). Adhering to these structural changes, the protein proceeded to different degrees of polymerization. BSA would aggregate into a high molecular mass (over 700 kDa) of protein ensemble when it was exposed to the mixed urea/DTT solution. An irreversible change in S–S/S–H conversion and secondary structure was responsible for protein misfolding. We demonstrate here that Fourier transform–Raman directly probe S–S/S–H conversion and secondary structural change of BSA at different states, and these results clearly indicate that disulfide bonds and secondary structure of BSA serve as concrete frameworks to stabilize protein structure. As the frameworks collapse, the protein undergoes an irreversible structural change and results in protein misfolding. Copyright © 2016 John Wiley & Sons, Ltd.     

High flow-resolution for mobility estimation in 2D-ENMR of proteins using maximum entropy method (MEM-ENMR)

Multidimensional electrophoretic NMR (nD-ENMR) is a potentially powerful tool for structural characterization of co-existing proteins and protein conformations. By applying a DC electric field pulse, the electrophoretic migration rates of different proteins were detected experimentally in a new dimension of electrophoretic flow. The electrophoretic mobilities were employed to differentiate protein signals. In U-shaped ENMR sample chambers, individual protein components in a solution mixture followed a cosinusoidal electrophoretic interferogram as a function of its unique electrophoretic migration rate. After Fourier transformation in the electrophoretic flow dimension, the protein signals were resolved at different resonant frequencies proportional to their electrophoretic mobilities. Currently, the mobility resolution of the proteins in the electrophoretic flow dimension is limited by severe truncations of the electrophoretic interferograms due to the finite electric field strength available before the onset of heat-induced convection. In this article, we present a successful signal processing method, the Burg's maximum entropy method (MEM), to analyze the truncated ENMR signals (MEM-ENMR). Significant enhancement in flow resolution was demonstrated using two-dimensional ENMR of two protein samples: a lysozyme solution and a solution mixture of bovine serum albumin (BSA) and ubiquitin. The electrophoretic mobilities of lysozyme, BSA and ubiquitin were measured from the MEM analysis as 7.5x10(-5), 1.9x10(-4) and 8.7x10(-5) cm2 V-1 s-1, respectively. Results from computer simulations confirmed a complete removal of truncation artifacts in the MEM-ENMR spectra with 3- to 6-fold resolution enhancement.     

Electronic band structure and Fermi surface of CaB6 studied by angle-resolved photoemission spectroscopy

We report high-resolution angle-resolved photoemission spectroscopy (ARPES) on CaB6. The band structure determined by ARPES shows a 1 eV energy gap at the X point between the valence and the conduction bands. We found a small electron pocket at the X point, whose carrier number is estimated to be (4-5) x 10(19) cm(-3), in good agreement with the Hall resistivity measurement with the same crystal. The experimental results are discussed in comparison with band structure calculations and theoretical models for the high-temperature ferromagnetism.     

尼古丁与BSA相互作用的光谱研究

用紫外-可见光谱和荧光光谱研究了尼古丁与牛血清白蛋白(bovine serum albumin, BSA)的相互作用。荧光研究表明,尼古丁浓度的增加引起BSA 345 nm处荧光有规律地猝灭。Stern-Volmer 方程分析pH 5.0,pH 7.4和pH 11.0体系的荧光猝灭机理发现,pH 5.0体系属动态猝灭,而pH 7.4和pH 11.0体系为静态猝灭。Lineweaver-Burk双倒数方程计算pH 7.4和pH 11.0体系在温度为20和37 ℃条件下尼古丁和BSA的结合常数k分别为：k_{20 ℃}=140.15 L·mol-1 ,k_{37 ℃}=131.83 L·mol-1 (pH 7.4)和k_{20 ℃}=141.76 L·mol-1,k_{37 ℃}=27.79 L·mol-1(pH 11.0),表明结合常数在pH 7.4条件下受温度的影响要比pH 11.0条件下小,推测是由于不同pH下尼古丁存在的不同形态所致。紫外-可见光谱研究表明,pH 7.4条件下尼古丁浓度的增加引BSA在210 nm处吸收峰吸收强度减小且红移,说明BSA二级结构发生变化,即螺旋结构变松散;紫外二阶导数光谱和同步荧光光谱(Δλ=λ_em-λ_ex=15 nm和Δλ=λ_<i>em-λ_ex=60 nm)分析尼古丁对BSA芳香性氨基酸(Trp, Tyr和Phe)残基微环境的变化,结果表明高浓度的尼古丁使所有这些芳香性氨基酸残基微环境由疏水环境转变为亲水环境。     

Probing the Interaction of Trans-resveratrol with Bovine Serum Albumin: A Fluorescence Quenching Study with Tachiya Model

The interaction of trans-resveratrol (TRES) and bovine serum albumin (BSA) was investigated using fluorescence spectroscopy (FS) with Tachiya model. The binding number maximum of TRES was determined to be 8.86 at 293.15 K, 23.42 at 303.15 K and 33.94 at 313.15 K and the binding mechanism analyzed in detail. The apparent binding constants (K (a)) between TRES and BSA were 5.02 x 10(4) (293.15 K), 8.89 x 10(4) (303.15 K) and 1.60 x 10(5) L mol(-1) (313.15 K), and the binding distances (r) between TRES and BSA were 2.44, 3.01, and 3.38 nm at 293.15, 303.15, and 313.15 K, respectively. The addition of TRES to BSA solution leads to the enhancement in RLS intensity, exhibiting the formation of the aggregate in solution. The negative entropy change and enthalpy change indicated that the interaction of TRES and BSA was driven mainly by van der Waals interactions and hydrogen bonds. The process of binding was a spontaneous process in which Gibbs free energy change was negative.     

新型水溶性花菁双嵌染料荧光测定蛋白质的研究

基于蛋白质对双嵌花菁染料具有良好的荧光增强作用,以新型水溶性碳菁染1,1’-丙磺酸-3,3,3’,3’-四甲基吲哚三次甲基碳菁-5,5’-二磺酸钾为荧光探针,建立了一种新的蛋白质荧光检测体系。实验考察了探针的荧光特征、浓度、缓冲体系pH、盐浓度和乙醇有机试剂等参数对体系荧光的影响。当pH2.0,花菁染料最大荧光激发波长为548 nm,发射波长为562 nm,血清蛋白与探针作用随着探针浓度的增加而加强,荧光增强值逐渐上升;当探针浓度为1.00×10-6mol·L-1时,牛血清蛋白BSA和人血清蛋白HSA对花菁探针荧光增强作用最为明显,体系荧光强度与蛋白质浓度成良好的线性关系,BSA和HSA线性响应浓度范围分别为0.20～15.00μg·mL-1和0.20～12.00μg·mL-1, 检测限(3σ/K)为0.01μg·mL-1。测定了血清蛋白BSA的合成样品,当BSA浓度为4.00,6.00,8.00μg·mL-1时,回收率为94.5%～103.3%。     

间二羧基苯氧基取代酞菁锌与白蛋白共价结合物的合成与光谱性质

制备了四种由β-四(3,5-二羧基苯氧基)酞菁锌(记为1)和β-八(3,5-二羧基苯氧基)酞菁锌(记为2)与人血清白蛋白(HSA)或牛血清白蛋白(BSA)构成的共价结合物,结合物中酞菁与白蛋白的摩尔组成比为6～7:1.在PBS溶液中的电子吸收光谱测试表明,当酞菁1共价结合到白蛋白上后,呈现出更明显的单体特征吸收(单体特...     

温度对鱼鳞胶原蛋白二级结构的影响

从草鱼鱼鳞中提取酶溶性胶原蛋白(PSC),通过SDS-PAGE电泳分析为典型Ⅰ型胶原蛋白且达到电泳纯。在此基础上利用傅里叶变换红外光谱(FTIR)、拉曼光谱(Raman)和圆二色谱(CD)研究了温度对鱼鳞胶原蛋白二级结构的影响。FTIR分析表明：鱼鳞胶原蛋白具有典型的胶原蛋白特征吸收带,酰胺Ⅰ、酰胺Ⅱ和酰胺Ⅲ带的特征吸收频率分别出现在1658,1552和1238cm-1处。随温度升高,酰胺A和酰胺B峰位向低波数移动,1658cm-1处吸收峰裂解成多个吸收峰;1552cm-1处的吸收峰在35℃微略红移,随后发生明显蓝移;1238cm-1处吸收峰随温度升高向低波数移动。在拉曼光谱中,胶原蛋白的酰胺Ⅰ、酰胺Ⅱ和酰胺Ⅲ带的特征吸收频率分别出现在1669,1557和1245cm-1处,都较红外光谱的波数高;此外,921和855cm-1处脯氨酸的特征谱峰在拉曼光谱中体现出来。圆二色谱分析表明,胶原蛋白溶液在221.6和204.4nm分别有一正、负峰,具有典型胶原蛋白三螺旋结构的特征圆二色谱峰型。胶原蛋白冻干品的FTIR光谱和Raman谱线大都在35～60℃时发生波数和强度改变,而胶原蛋白乙酸溶液的CD谱线在20～35℃之间发生剧烈改变。由此可以判断胶原蛋白在固态和溶液状态下,变性温度存在一定差异,胶原蛋白冻干品比其乙酸溶液更稳定。     

吲哚基二聚体菁类探针同步荧光测定蛋白质的研究

基于蛋白质对双嵌吲哚染料具有良好的荧光增强作用,以新型水溶性吲哚基同型二聚体探针I,建立了一种灵敏的蛋白质同步荧光分析体系。实验考察了吲哚探针的荧光特征、吲哚探针浓度、缓冲体系pH、盐浓度等参数对体系荧光的影响。在酸性条件下,蛋白质分子与探针I发生结合作用,同步荧光明显增强并向长波方向发生红移,且同步荧光强度与蛋白质浓度成良好的线性关系。在最优条件下,牛血清白蛋白BSA的线性响应范围5.00×10-7～2.50×10-5 g·mL-1,检测限(3σ/K)为3 ×10-8 g·mL-1;测定了血清蛋白BSA的合成样品,不同浓度BSA样品回收率为98.6%～103.0%,相对标准偏差1.1%～1.9%;与蛋白质紫外标准测定法比较,测定偏差为0.4%～3.9％。     

Fourier Transform Infrared Emission Spectroscopy of SeH

The infrared vibration-rotation bands of SeH have been measured in the X(2)Pi ground state using a Fourier transform spectrometer. The bands were observed in a microwave discharge of a mixture of H(2) and Se in the presence of He. The rotational structure of the 1-0, 2-1, 3-2 bands of the X(2)Pi(3/2) spin component and the 1-0 band of X(2)Pi(1/2) spin component has been observed in the 1800-2600 cm(-1) region. The principal ground state molecular constants obtained are omega(e) = 2421.7153(234) cm(-1), omega(e)x(e) = 44.6012(110) cm(-1), omega(e)y(e) = 0.20697(236) cm(-1), B(e) = 7.899187(696) cm(-1), alpha(e) = 0.220749(399) cm(-1), and r(e) = 1.464319(64) ?. This work is the first determination of the equilibrium molecular constants of the X(2)Pi state of SeH. Copyright 2000 Academic Press.