関連する実験動画

Updated: Oct 25, 2025

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
08:34

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

6.9K

Amphiphilic Polymer Folding beyond the Primary Structure with Protein-Mimetic Di(Phenylalanine) を制御する タンパク質を模倣する

Jacqueline L Warren1, Peter A Dykeman-Bermingham1, Abigail S Knight1

  • 1Department of Chemistry, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, United States.

Journal of the American Chemical Society
|August 10, 2021
PubMed
まとめ

合成ポリマーは非共性相互作用を組み込むことでタンパク質の機能を模倣することができます. この研究は,ディフェニララリン) アクリルアミドのような特定のモノメアの設計が,合成ポリマーで秩序あるタンパク質のような構造の形成を可能にすることを示しています.

さらに関連する動画

Controlling the Size, Shape and Stability of Supramolecular Polymers in Water16:24

Controlling the Size, Shape and Stability of Supramolecular Polymers in Water

Published on: August 2, 2012

18.9K
Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides07:26

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

Published on: November 21, 2013

13.1K

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...
9.8K
Protein Folding01:22

Protein Folding

Overview
123.7K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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...
18.8K
Protein Organization01:13

Protein Organization

Overview
150.6K
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....
8.1K
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,...
10.9K