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関連する概念動画

Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein Folding

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 Fibrils03:03

Amyloid Fibrils

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, normally used to...
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Protein Organization01:13

Protein Organization

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Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...

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Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
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折りたたみ構造は,協和結合マクロ分子によって構成される.

Koushik Ghosh1, Jeffrey S Moore

  • 1Department of Chemistry and the Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.

Journal of the American Chemical Society
|November 17, 2011
PubMed
まとめ
この要約は機械生成です。

メタフェニレンエチニレン (mPE) 折りたたみに付着した大きなマクロモレキュルは,それらを螺旋構造に崩壊させる. この折りたたみ効果は,より大きなマクロ分子でより顕著であり,本質的に構造化されていないタンパク質の洞察を提供します.

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09:34

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

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科学分野:

  • ポリマー化学のポリマー化学について
  • バイオフィジックス 生物物理学
  • マクロ分子科学 マクロ分子科学

背景:

  • 本質的に構造化されていないタンパク質 (IUP) は,他のタンパク質と相互作用し,影響することによって,細胞環境で重要な役割を果たします.
  • 折りたたみ物質は,特定の形状を採用するように設計された合成ポリマーであり,生物学的マクロモレキュルのモデルとして機能します.

研究 の 目的:

  • メタフェニレンエチニレン (mPE) オリゴマーの構造折りたたみに対する付着マクロ分子の影響を調査する.
  • mPE折り畳み材料におけるマクロ分子誘発折り畳みの分子量依存性を調査する.
  • IUPの物理を研究するためのモデルシステムとして,mPEの折り畳み器を確立する.

主な方法:

  • 光スペクトロスコピーは,形状の変化をモニタリングするために使用されました.
  • 電子吸収スペクトロスコピーは,コンフォームに関連した電子特性を分析するために使用されました.
  • 添付されたマクロモレキュルのサイズが異なるmPEデデカメアで実験が行われました.

主要な成果:

  • mPEドデカメアの両端に付着したマクロモレキュルは,推定される螺旋状の形状に崩壊を誘導します.
  • 折りたたみ効果は,マクロモレキュルのセグメントが約50 kDa を超えたときに著しく強化されました.
  • 適合構造は,十分に大きなマクロ分子が付着した溶媒のデナチュレーションにおいてさえ観察された.

結論:

  • チェーン中心の折りたたみ器は,外部マクロ分子によって折りたたみさせられ,IUP行動の側面を模倣することができます.
  • 誘導マクロモレキュルの大きさは,折り畳み器の崩壊の程度を決定する重要な要因です.
  • これらの発見は,固有の非構造タンパク質に関する基礎研究のためのモデルシステムとして,foldamersの有用性をサポートしています.