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首页> 外文期刊>Biochemistry >Effects of Disulfide Bonds on Compactness of Protein Molecules Revealed by Volume, Compressibility, and Expansibility Changes during Reduction.
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Effects of Disulfide Bonds on Compactness of Protein Molecules Revealed by Volume, Compressibility, and Expansibility Changes during Reduction.

机译：二硫键对蛋白质分子紧实度的影响，可以通过还原过程中的体积，可压缩性和可膨胀性变化来揭示。

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摘要

To elucidate the effects of disulfide bonds on the compactness of protein molecules, the partial specific volume (vmacr; degrees ) and coefficients of adiabatic compressibility (beta(s) degrees ) and thermal expansibility (alpha) of five globular proteins (ovalbumin, beta-lactoglobulin, lysozyme, ribonuclease A, and bovine serum albumin) were measured in aqueous solutions with pH values of 7 and 2 at 25 degrees C when their disulfide bonds were totally reduced by carboxamidomethylation. Circular dichroism and fluorescence spectra show that the secondary and tertiary structures are partly disrupted by reduction, depending on the number of disulfide bonds in the proteins and the pH of the medium. The conformational changes are accompanied by decreases in vmacr; degrees and beta(s) degrees and by an increase in alpha, indicating that reduction decreases the internal cavity and increases surface hydration. The beta(s) degrees values of native or oxidized proteins decrease, and the effects of reduction on the volumetric parameters become more significant as the number of disulfide bonds increases and as they are formed over a larger distance in the primary structure. These results demonstrate that disulfide bonds play an important role, mainly via entropic forces, in the three-dimensional structure and compactness of protein molecules.
机译：为了阐明二硫键对蛋白质分子，部分比容（vmacr;度）和绝热压缩系数（beta（s）度）和热膨胀系数（alpha）的五个球形蛋白质（卵清蛋白，β-在25℃下，当其二硫键通过羧酰胺甲基化完全还原时，在pH值为7和2的水溶液中测量乳球蛋白，溶菌酶，核糖核酸酶A和牛血清白蛋白）。圆二色性和荧光光谱表明，二级和三级结构被还原部分破坏，这取决于蛋白质中二硫键的数量和培养基的pH值。构象变化伴随着vmacr的减少;度和β度，以及α的增加，表明减少会减少内部空腔并增加表面水合作用。天然或氧化蛋白的β值降低，并且随着二硫键数量的增加以及在一级结构中形成的距离更长，还原对体积参数的影响变得更加明显。这些结果表明，二硫键主要通过熵力在蛋白质分子的三维结构和紧密度中起重要作用。

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