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Protein Folding01:22

Protein Folding

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Overview
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Protein Folding01:25

Protein Folding

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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...
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Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Protein and Protein Structure02:15

Protein and Protein Structure

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
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Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

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Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
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Single-Strand DNA Binding Proteins01:03

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For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
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H-ボンドの自己組み立て:折りたたみ対複合形成

Diego Núñez-Villanueva1, Giulia Iadevaia1, Alexander E Stross1

  • 1Department of Chemistry, University of Cambridge , Lensfield Road, Cambridge CB2 1EW, U.K.

Journal of the American Chemical Society
|May 5, 2017
PubMed
まとめ
この要約は機械生成です。

H結合部位を持つオリゴーマーが複合体または折りたたみを形成する. 頑丈な脊椎は複合体を好み 合成情報分子を可能にしますが 柔軟な脊椎は折り畳み 弱い複合体を形成します

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科学分野:

  • 超分子化学
  • 化学生物学
  • 有機化学

背景:

  • 水素結合ドナー部位 (D) と受容体部位 (A) を有する線形オリゴーマーが複合体または折りたたみを形成する.
  • 分子間複合形成と 分子内折り合いの間の競合する均衡は 分子組成に影響する.

研究 の 目的:

  • 様々なオリゴマー系における複合形成と折り畳みの競合する均衡を定量化する.
  • 骨幹の柔軟性と認識サイトの設計が自己組み立てに与える影響を調査する.

主な方法:

  • 7つの異なるオリゴーマー構造を研究するために,NMRの定位と稀縮実験が採用された.
  • 分析は自己関連定数を定量化し,支配的な折り畳みまたは二重形成経路を特定することに焦点を当てました.

主要な成果:

  • ホモシーケンスのダイマー (AA·DD) は,競合する折りたたみなしに一貫して二重構造を形成する.
  • ヘテロシーケンスのジマー (AD) は二重形成を示したが,柔軟な脊椎系におけるモノメアの折りたたみにより安定性が低下した.
  • 柔軟な背骨 (≥5回転結合) は,分子内H結合を好み,二重結合の安定性を1〜2度減少させた.
  • 固い背骨 (<5回転結合) は分子内相互作用を防止し,安定した二重結合形成を可能にしました.

結論:

  • 競争する折り畳みバランスを防止し,安定した分子間相互作用を可能にするために,脊椎の硬さは極めて重要です.
  • 硬い脊椎を持つオリゴーマーには 長い配列選択性合成情報分子を 開発する可能性がある.
  • これらの競合するバランスを理解することは 機能的な超分子システムを設計する上で鍵となるものです