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Folding intermediate of beta -lactoglobulin with non-native alpha -helical conformation

机译:具有非天然α的β-裂藻蛋白的折叠中间体 - Helical兼容

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Protein folding is a process in which a polypeptide chain attains a unique native structure that is determined by its amino acid sequence. Several mechanisms have been proposed to explain the efficient folding process of globular proteins. In particular, a sequential and hierarchical folding mechanism with a molten globule intermediate has been popular [1]. In contrast, a nucleation/condensation model of protein folding has been recently evaluated, in which the rate-limiting step is the formaiton of a nucleus [2]. In both models, it is generally considered that the intermediate conformational states assume the native-like substructures (hierarchical mechanism of folding).
机译:蛋白质折叠是一种过程,其中多肽链达到独特的天然结构,其由其氨基酸序列测定。已经提出了几种机制来解释球状蛋白的有效折叠过程。特别地,具有熔融小球中间体的顺序和分层折叠机构已经受欢迎[1]。相反,最近已经评估了蛋白质折叠的成核/缩合模型,其中速率限制步骤是核[2]的形式分子。在这两种模型中,通常认为中间构象状态呈现类似地形子结构(折叠的分层机制)。

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