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Updated: Jun 14, 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

分子構造を通してペプチド繊維の超分子剛性を調節する

E Thomas Pashuck1, Honggang Cui, Samuel I Stupp

  • 1Department of Materials Science and Engineering, Northwestern University, Evanston, Illinois 60208, USA.

Journal of the American Chemical Society
|April 10, 2010
PubMed
まとめ

科学者は,アミノ酸配列を変更することによって,ペプチドアンフィフィール (PA) ナノファイバーを設計しました. ヴァリンの付加はゲルの硬さを増加させ,アラニンはそれを減少させ,バイオマテリアルの特性に対する制御を提供した.

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Protein Folding01:25

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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.
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Protein Organization01:24

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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.
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A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...