水溶性生物模倣折り畳み器の再折り畳み
PubMedで要約を見る
まとめ
この要約は機械生成です。研究者は内部非共性相互作用を緩和して構造を変更する新しいダイナミックな折り畳み器を設計しました この突破は刺激反応性物質と 分子機械の 新しい設計戦略を提供します
科学分野
- 超分子化学
- 材料科学
- バイオ物理学
背景
- 挫折した,または非最適の相互作用は,タンパク質の反応性 (アロステリー,シグナル伝達) に極めて重要です.
- 動的折り畳み器の設計要素として挫折した非共性相互作用の使用は未知のままです.
研究 の 目的
- 水溶性折りたたみ器を設計し合成し 構造の再編成のために 挫折の解消を活用しました
- 非共性ネットワークの変化によって引き起こされる刺激反応の行動を調査する.
主な方法
- 新しい動的折り畳み器の設計と合成
- 顕微鏡と構造技術を用いた特徴付け.
- 構造的移行とエネルギー的な駆動力を分析する分子ダイナミクスシミュレーション
主要な成果
- 水溶性ダイナミック折り畳み器の成功設計と合成
- 刺激に対する反応として,折りたたみ構造から交差した柱状構造への構造的再配置が示されている.
- 構造変化のエネルギー的な原動力として特定された 挫折の緩和
結論
- 刺激に反応するダイナミックな折りたたみを作るのに有効な設計要素です.
- このアプローチは先進的な材料や 合成生物学ツールや 分子機械の開発に 新たな道を開きます
関連する概念動画
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...

