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関連する概念動画

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...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:22

Protein Folding

Overview
Protein Organization01:13

Protein Organization

Overview
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.
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...

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関連する実験動画

Updated: May 21, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

ペプチド折合体における核化の効果

Anupam Patgiri1, Stephen T Joy, Paramjit S Arora

  • 1Department of Chemistry, New York University, New York, New York 10003, USA.

Journal of the American Chemical Society
|June 22, 2012
PubMed
まとめ

ベータ (((3) - アミノ酸オリゴーマーが,アルファヘリクスの安定した構造的模倣を提供している. これらの異質な配列は,マクロサイクルテンプレッティングの影響を受けたアルファペプチドヘリクと比較して,構造的硬直性が増加しています.

科学分野:

  • バイオケミストリー バイオケミストリー
  • 有機化学 オーガニック・ケミストリー
  • 構造生物学 構造生物学とは

背景:

  • ベータ(3) - アミノ酸のオリゴーマーおよび混合アルファ/ベータ(3) - 残基は,アルファヘリクスのタンパク質分解的に安定した構造的模倣物です.
  • これらのオリゴマーは,短いシーケンスでも,定義された形状を採用することができます.

研究 の 目的:

  • 核前ヘリコプターにおけるアルファアミノ酸類似体と比較したベータ3残留物の影響を評価する.
  • ベータ3残基を含む異質な配列の構成性質を調査する.

主な方法:

  • 水素-デウテリウム交換実験が採用されました.
  • アルファ-およびベータ-残基の異なる組成を持つプレヌクレアヘリクスの分析.

主要な成果:

  • "アルファ・アルファ・ベータ"の繰り返しを持つ異質な配列は,同質なアルファ-ペプチドヘリクよりも大きな形状の硬さを示した.
  • マクロサイクルの螺旋形状模様は,観測された硬さに大きな影響を与えた.

結論:

  • ベータ (((3)-残基は,螺旋性オリゴマーの形状の硬さを高めます.

さらに関連する動画

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets
13:42

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets

Published on: November 2, 2011

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
10:50

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

Published on: September 15, 2010

関連する実験動画

Last Updated: May 21, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets
13:42

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets

Published on: November 2, 2011

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
10:50

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

Published on: September 15, 2010

  • マクロサイクルの構造は,これらのアルファヘリックス模倣体の構造的安定性を決定する上で重要な役割を果たします.