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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >X-ray structure analysis of a designed olilgomeric miniprotein reveals a discrete quaternary architecture
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X-ray structure analysis of a designed olilgomeric miniprotein reveals a discrete quaternary architecture

机译：设计的寡聚小蛋白的X射线结构分析揭示了离散的四级结构

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摘要

The x-ray crystal structure of an oligomeric miniprotein has been determined to a 1.2-Angstrom resolution by means of multiwavelength anomalous diffraction phasing with selenomethionine analogs that retain the biophysical characteristics of the native peptide. Peptide 1, comprising alpha and beta secondary structure elements with only 21 aa per monomer, associates as a discrete tetramer. The peptide adopts a previously uncharacterized quaternary structure in which alpha and beta components interact to form a tightly packed and well defined hydrophobic core. The structure provides insight into the origins of the unusual thermal stability of the oligomer. The miniprotein shares many characteristics of larger proteins, including cooperative folding, lack of 1-anilino-8-naphthalene sulfonate binding, and limited deuterium exchange, and possesses a buried surface area typical of native proteins.
机译：寡聚小蛋白的X射线晶体结构已通过硒代蛋氨酸类似物的多波长异常衍射定相，确定了1.2埃的分辨率，而硒代蛋氨酸类似物保留了天然肽的生物物理特性。包含每个单体仅具有21aa的α和β二级结构元素的肽1缔合为离散的四聚体。该肽采用以前未表征的四级结构，其中α和β成分相互作用形成紧密堆积且界限分明的疏水核心。该结构提供了对低聚物异常热稳定性起源的洞察力。小蛋白具有较大蛋白的许多特征，包括协同折叠，缺乏1-苯胺基-8-萘磺酸盐的结合以及有限的氘交换，并且具有天然蛋白特有的掩埋表面积。

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