氨基酸从水到尿素水溶液中的迁移焓研究

用微量量热法测定甘氨酸、L-丙氨酸、L-丝氨酸在水和尿素水溶液中的溶解焓, 计算得到氨基酸从水到尿素水溶液的迁移焓, 并根据水合结构相互作用模型予以讨论. 结果表明, 氨基酸两性离子与尿素分子的静电作用以及两性离子头部与尿素分子的结构相互作用对氨基酸迁移焓有负贡献, 氨基酸侧链与尿素分子的结构相互作用依其亲水性或疏水性分别对迁移焓有负贡献或正贡献. 在实验浓度范围(0～13 mol/kg)内, 三种氨基酸的迁移焓总体上随尿素浓度的增加而下降, 其大小依次为L-丝氨酸＜甘氨酸＜L-丙氨酸, 氨基酸迁移焓的差异反映了溶质-溶剂结构相互作用的变化.     

水溶液中氨基酸与甲脲的焓相互作用

用LKB-2277精密微热量计测定了298.15 K时甘氨酸、L-丙氨酸、L-丝氨酸、L-缬 氨酸、L-苏氨酸和L-脯氨酸六种α-氨基酸分别与甲脲分子在水溶液中的混合过程焓变及 这些溶质分子在水溶液中的稀释焓.实验数据根据McMillan-Mayer理论进行回归分析,得到 各级交叉焓相互作用系数.讨论了不同氨基酸与甲脲分子的相互作用机制.结果表明,氨基酸 的两性离子部分、α-碳上的非极性脂肪侧基、极性的羟基侧基和五元吡咯环结构对交叉焓 对作用系数hxy具有不同贡献.与尿素相比,甲脲分子中-CH3基团的引入明显增强了分子的 疏水性.     

三种氨基酸在尿素水溶液中的体积性质

精密密度法详细测定甘氨酸、L-丙氨酸、L-丝氨酸在尿素水溶液中的表观摩尔体积,计算了三种氨基酸从水到尿素水溶液的迁移偏摩尔体积,结合前期的氨基酸从水到尿素水溶液的迁移焓,探讨尿素水溶液的结构特点及其对氨基酸与尿素在水溶液中相互作用的影响。结果表明,尿素分子在水溶液中自缔合,引起溶剂结构的变化并削弱其与氨基酸分子的结构相互作用,造成氨基酸从水到尿素水溶液的迁移偏摩尔体积和迁移焓随尿素浓度的增加而出现多个变化点,这一效应随着氨基酸疏水性的增强而增大,表明氨基酸的疏水性越强,其与尿素相互作用引起的去水化作用越明显。     

甘氨酸与氯化碱金属在水中的焓相互作用参数

氨基酸在混合溶液中的热力学性质及相互作用的研究不论对溶液化学还是生命科学都是十分重要的．对此国内已有不少的研究h，’1．利用偿效应的方法研究氨基酸与电解质间的相互作用是很有效的卜一句，但大多数的工作都是在低浓度下研究一个氨基酸分子和一个电解质离子对间的相互作用烩．本文测定了甘氨酸在水中和在LICI、NaCI、KCI的水溶液中的溶解偿，计算出甘氨酸与各个公在水中的偿对相互作用参数和三相互作用参数，并由此讨论了甘氨酸与这些盐的对分子相互作用和三分子相互作用．1实验部分试剂：甘氨酸为ARfa，K甲醇一水重结晶．LI…     

甘氨酸在氯化钾水溶液中的稀释焓

利用瑞典LKB-2277生物活性检测仪测定了298．15K时甘氨酸在不同浓度的氯化钾水溶液中的稀释焓,根据McMilkm-Mayer理论计算了甘氨酸在不同浓度的氯化钾水溶液中的同系焓相互作用系数．结果表明,甘氨酸在氯化钾水溶液中的焓对相互作用系数h2均为负值,并且随着氯化钾浓度的增加,h2的绝对值逐渐减小。     

氨基酸在水/DMF混合溶剂中的焓相互作用

氨基酸是组成蛋白质的基本结构单位。溶质－溶质相互作用是氨基酸溶液热力学性质研究的一个主要方面，氨基酸的稀释焓是与之相应的一个重要热力学性质。目前，研究多集中在水溶液中，研究表明具有非极性侧链氨基酸和具有极性侧链氨基酸的偏摩尔焓是完全不同的，随着氨基酸...     

肌醇在氯化钠水溶液中的稀释焓和焓对相互作用

应用微量热法测定了298.15K时肌醇在纯水和氯化钠水溶液中的稀释焓,根据McMillan-Mayer理论计算了肌醇在不同浓度的氯化钠溶液中的2到4阶焓相互作用系数.结果表明,肌醇在氯化钠溶液中的焓对相互作用系数h2均为负值,并且随着氯化钠浓度的增大,h2的值呈增大趋势.根据溶质-溶质相互作用和溶质-溶剂相互作用对焓对相互作用系数的变化趋势进行了解释.     

三种氨基酸从水到DMSO水溶液的迁移焓研究

用微量量热法测定甘氨酸、L-丙氨酸、L-丝氨酸在二甲基亚砜(DMSO)水溶液中的溶解焓, 计算得到三种氨基酸从水到DMSO水溶液的迁移焓, 根据共球交盖模型对氨基酸与DMSO在水溶液中的相互作用进行讨论, 并与前期的氨基酸在尿素水溶液体系中的迁移焓进行比较. 结果显示, 氨基酸与共溶剂分子之间产生的静电相互作用以及亲水-亲水相互作用对氨基酸迁移焓有负贡献, 而亲水-疏水、疏水-疏水相互作用对氨基酸迁移焓有正贡献. 与尿素水溶液中氨基酸迁移焓的绝对值随尿素浓度的增加而增加, 并规律性地出现多个变化点的情况不同, 氨基酸从水到DMSO水溶液的迁移焓随DMSO浓度的增加而线性增加. 这种差异反映了尿素与DMSO及其水溶液结构的不同, 为认识尿素在水溶液中的缔合作用提供了对比依据.     

丝氨酸在醇-水溶液中的溶解焓

用RD-496III双热流精密微热量计测量了L-丝氨酸在纯水以及异丙醇、1,2-丙二醇和丙三醇水溶液中的溶解焓, 并计算了从水到醇-水溶液中的迁移焓. 实验发现, L-丝氨酸在水及醇-水溶液中的溶解焓都是正值, 它从水到醇-水溶液中的迁移焓也都是正值, 并且基本上随着醇浓度的增加而增加, 说明在溶解过程中, 溶质与混合溶剂分子的部分去水化吸热过程占主要地位. 另外, 实验还发现L-丝氨酸从水到异丙醇水溶液中的迁移焓大于在1,2-丙二醇水溶液中的, 更大于在丙三醇水溶液中的, 这是由于羟基的减少导致了疏水-亲水作用的增加和亲水-亲水作用的减弱.     

Enthalpic interactions between some amino acids and cyclohexanone in aqueous solutions at 298.15 K

The enthalpies of mixing of glycine, l-α-alanine, l-γ-aminobutyric acid, l-α-valine, l-α-serine and l-α-threonine with cyclohexanone in aqueous solutions and their respective enthalpies of dilution have been measured by calorimetry at 298.15 K. Experimental enthalpies of dilution and mixing have been correlated with the virial expansion equation that was obtained with the McMillan-Mayer theory. The enthalpic interaction parameters h_xy, h_xxy and h_xyy of the amino acids studied with cyclohexanone in aqueous solutions have been evaluated, and the heterotactic enthalpic pair interaction coefficients (h_xy) are discussed in terms of solute-solute interactions.     

Interactions between terminally substituted amino acids in an aqueous and a non-aqueous environment. Enthalpic interaction coefficients in water and in N,N-dimethylformamide at 25°C

Enthalpies of dilution of the N-acetyl amides of glycine, L-alanine, L-valine, L-leucine, and L-phenylalanine, dissolved in N,N-dimethylformamide (DMF) as a solvent have been measured at 25°C. The results obtained have been analyzed to give the enthalpic interaction (or virial) coefficients of the solutes and these are compared with information previously obtained in aqueous systems. There are marked differences in the interaction properties in the two solvents and, while the additivity approach of Savage and Wood is applicable to the solutes in water it is not suitable for representing the interactions in DMF. A correlation is presented between the enthalpic second virial coefficients in DMF and the propensity of side-chains to be in proximity in globular proteins.     

A study of solute-solute interactions of amides dissolved in N-methylformamide by enthalpic interaction coefficients

Enthalpies of dilution of formamide, acetamide, propionamide, butyramide and hexanamide, dissolved in N-methylformamide have been measured calorimetrically at 25°C. From the results McMillan-Mayer coefficient related enthalpic pair and triplet interaction coefficients have been calculated. Except for those of formamide, all pair coefficients are negative, whereas the triplet terms are positive. The values in the protic solvent N-methylformamide presented in this paper together with those published before are compared with results for corresponding solutes dissolved in the aprotic solvent N,N-dimethylformamide. A discussion of the dependence of the interaction coefficients on the applied concentration scale is given and conversion factors are presented. The influence of hydrogen bonding, of substituent effects on this hydrogen bonding, and of polarophobic interaction is discussed. The latter is comparable in N,N-dimethyl-and N-methylformamide. The enthalpic pair interaction coefficients have been correlated with the Excess Group Additivity approach.To whom correspondence should be addressed.     

α-氨基酸-丁醇-水三元体系中分子间的异系焓相互作用

利用2277热活性检测仪的流动测量系统获得了298.15K时甘氨酸、L-丙氨酸、L-缬氨酸和L-脯氨酸分别与n-丁醇在水溶液中混合过程的焓变以及各自的稀释焓,依据McMillan-Mayer理论关联得到异系焓相互作用系数,讨论了不同氨基酸与n-丁醇分子的作用机理.对hxy值分析结果表明,不同氨基酸与n-丁醇分子间的异系焓作用系数的大小主要取决于氨基酸分子结构的差异,氨基酸的不同侧基(非极性或极性)对焓作用系数有着不同的贡献,焓作用系数值的相对大小最终取决于各基团之间竞争平衡的结果.脯氨酸特殊的五元吡咯环结构对hxy值有较大的正贡献;n-丁醇的疏水性比尿素或甲脲大得多.     

Physicochemical investigation on interactions of some amino acids with aqueous tetra-butyl ammonium bromide solution at 298.15 K

Apparent molar volumes, viscosity B-coefficients, and apparent molar isentropic compressibilities of glycine, L-alanine, L-valine and L-leucine in 0.062, 0.125 and 0.256 mol kg^?1 aqueous tetra-butyl ammonium bromide (TBAB) solution have been determined at 298.15 K from their experimental density, flow time and sound speed measurements, respectively. The standard partial molar volumes and compressibilities are used to calculate the corresponding volume of transfer at infinite dilution, from water to aqueous TBAB solutions. The linear correlation of partial molar volumes for a homologous series of amino acids has been utilised to calculate the contribution of charged end groups and other alkyl chains of the amino acids to partial molar volumes. The hydration numbers of amino acids have also been determined. Viscosity B-coefficients have been calculated using the Jones–Dole equation. The values of the charged end groups contribution to the viscosity B-coefficients of the amino acids are calculated.     

Enthalpies of dilution and homotactic enthalpic interaction coefficients of THF and 1,4-dioxane at 298.15 k

Enthalpies of dilution at 298.15 K of aqueous solutions of THF and 1,4-dioxane have been determined using flow microcalorimetry. The results obtained were used to determine the homotactic enthalpic interaction coefficients that characterize pair interactions of THF and 1,4-dioxane in aqueous solution. These are briefly discussed from the point of view of intermolecular interaction between the hydrated solute species.     

The enthalpies of dilution of pyridine and methylpyridine at 298.15 K

The enthalpies of dilution of aqueous solutions for pyridine and methylpyridine isomers have been determined with a 2277-Thermal Activity Monitor at 298.15 K. The results have been treated using the excess function concept and homotactic interaction coefficients have been obtained. The homotactic enthalpic pairwise interaction coefficients are discussed qualitatively in terms of substitution effects of methyl group introduced into the pyridine ring.     

The aromatic amino acid behaviour in aqueous amide solutions

The enthalpies of solution of L-phenylalanine in the mixtures of water with the protein denaturant urea have been measured in the temperature range of 288.15–318.15 K. Using the results of the present research and literature data of free energies, the standard thermodynamic functions of the solute transfer from water to aqueous urea solutions have been estimated in a wide temperature range. The enthalpic, heat capacity, entropic and free energy parameters of the solute-urea pair and triplet interactions have been computed. The amino acid — amide pair interaction was found to be attractive in the temperature range studied due to the favourable enthalpic term. The triplet interaction being slightly repulsive reveals the enthalpic origin also. The examination of the Savage and Wood additivity-of-groups approach does indicate the inapplicability of this scheme to enthalpies and entropies of interaction. It has been found for the first time that the heat capacity of interaction changes its sign at 303 K, i.e. the temperature dependence of enthalpic and entropic parameters passes through the pronounced extrema near the temperature of the minimum of the heat capacity of pure water.     

Aqueous solutions containing amino acids and peptides. Part 19: The enthalpic coefficients for the interactions of N-acetylsarcosinamide with 2-(N-acetylamino)acyl amides at 25°C

Enthalpies of dilution both of solutions of N-acetylsarcosinamide and of ternary solutions equimolal in N-acetylsarcosinamide and N-acetylglycinamide, N-acetyl-L-alaninamide, N-acetyl-L-valinamide or N-acetyl-L-leucinamide have been determined by a microcalorimetric method. The results were employed to calculate the pairwise enthalpic coefficients for both homotactic (like-like) and heterotactic (like-unlike) solute interactions. These pairwise interaction coefficients have been analyzed by means of a group additivity approach and some comments on the utility of this, when applied to such systems, are made.     

Enthalpic Interactions of Amino Acids with Glucose in Aqueous Solutions at 298.15 K

The enthalpies of mixing of aqueous glucose solutions and six kinds of aqueous amino acid solutions (glycine, L-alanine, L-serine, L-valine, L-proline, and L-threonine) and their respective enthalpies of dilution have been determined at 298.15 K using flow microcalorimetry. The experimental data have been analyzed in terms of the McMillan–Mayer model to obtain the heterotactic interaction coefficients. The results have been interpreted from the point of view of solute–solute interactions.