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PROTEIN FOLDING AND CONFORMATIONAL DISEASES

机译：蛋白质折叠和整合性疾病

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The protein molecules take the shape of a globule in the aqueous environment. The spontaneous folding processes are explained broadly by two models, such as structural and kinetic. The structural models aim at the actual structure of intermediates which appear before the formation of dominant intermediates prior to the formation of native globular protein. The kinetic models emphasize on the formation of native globular protein as well as dominant intermediates and the rate of the folding process. Variants of kinetic models include biased random search, nucleation growth and sequential folding pathways. Structural models propose that 'H' bonded structures occupy the lowest position in the hierarchical order of the native protein formation pathway. Though the information necessary for the correct folding of polypeptide chain is nascent in the primary structure of polypeptide, still 15% of the globular proteins require the help of chaperones and chaeronins. Conformational diseases are a gorup of disorders, which share common molecular pathology. Each disease arises from the same destabilizing mutations and polymerization of conformationally unstable protein occurs intraceilularly at the site of synthesis leading to accumulation of protein aggregates, such as alpha, antitrypsin in hepatocytes and neurotropin in neurons. The intracellular polymer formation is common determinant of neurodegeneration in Inclusion body dementias such as spongiform encephalopathies, sporadic and familial Parkinson's disease and Alzheimer's disease. Similarly onset and severity of the hepatic cirrhosis is associated with the aggregation of alpha antitrypsin in hepatocytes. The challenge of the day is to design suitable diagnostic technique prior to the appearance of cellular inclusion body and develop suitable drug delivery system either to prevent the polymerization of aberrant protein or to increase the secretion of cellular protein aggregates.
机译：蛋白质分子在水性环境中呈球状。自发折叠过程由两种模型广泛解释，例如结构模型和动力学模型。结构模型针对中间体的实际结构，该中间体在天然球形蛋白形成之前在主要中间体形成之前出现。动力学模型强调天然球蛋白的形成以及主要的中间体和折叠过程的速率。动力学模型的变体包括偏向随机搜索，成核生长和顺序折叠途径。结构模型提出“ H”键结构在天然蛋白质形成途径的层次顺序中占据最低位置。尽管正确折叠多肽链所需的信息尚处于多肽的一级结构中，但仍有15％的球状蛋白需要伴侣蛋白和伴侣蛋白的帮助。构象疾病是一类疾病，它们具有共同的分子病理学。每种疾病都源于相同的破坏稳定突变，构象不稳定蛋白的聚合发生在合成位点的脑内，导致蛋白聚集体的积累，例如肝细胞中的α，抗胰蛋白酶和神经元中的神经营养蛋白。细胞内聚合物的形成是包涵体痴呆例如海绵状脑病，散发性和家族性帕金森氏病和阿尔茨海默氏病中神经退行性变的普遍决定因素。同样，肝硬化的发作和严重程度也与肝细胞中α抗胰蛋白酶的聚集有关。当今的挑战是在细胞包涵体出现之前设计合适的诊断技术，并开发合适的药物输送系统，以防止异常蛋白的聚合或增加细胞蛋白聚集体的分泌。

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