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関連する概念動画

Protein Complex Assembly02:41

Protein Complex Assembly

10.7K
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.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
10.7K
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

21.3K
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
21.3K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

5.9K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
5.9K
Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

1.9K
Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
1.9K
Cytoskeletal Accessory Proteins01:13

Cytoskeletal Accessory Proteins

3.2K
The cytoskeleton is an essential cell component that plays several structural and functional roles. However, the filaments that make up the cytoskeleton cannot function independently and depend on the accessory or ancillary proteins to effectively carry out their function. Accessory proteins associate with cytoskeletal filaments and their monomers, aiding filament formation and function. They also help in the cross-communication among cytoskeletal filaments. Cytoskeletal accessory proteins are...
3.2K
Amyloid Fibrils03:03

Amyloid Fibrils

9.7K
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,...
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Updated: Aug 28, 2025

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
05:58

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Published on: July 17, 2019

11.1K

幻覚を誘う シンメトリックなタンパク質組

B I M Wicky1,2, L F Milles1,2, A Courbet1,2,3

  • 1Department of Biochemistry, University of Washington, Seattle, WA, USA.

Science (New York, N.Y.)
|September 15, 2022
PubMed
まとめ
この要約は機械生成です。

ディープラーニングは 大型のリングを含む 新しく対称なタンパク質構造を 設計できます これらの生成されたタンパク質の設計は構造的に正確で バイオマテリアルとナノマシンの可能性を広げています

さらに関連する動画

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

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Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions
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Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions

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関連する実験動画

Last Updated: Aug 28, 2025

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
05:58

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Published on: July 17, 2019

11.1K
Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

15.5K
Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions
06:32

Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions

Published on: July 28, 2022

2.3K

科学分野:

  • 生物化学
  • 構造生物学
  • コンピュータ生物学

背景:

  • ディープラーニングのジェネラティブモデルは タンパク質の構造空間を 探求するための新しい道を開きます
  • 現在の方法は天然のタンパク質の配列と構造に限られている.

研究 の 目的:

  • ディープネットワークの幻覚を用いて 新種の対称タンパク質ホモオリゴーマーを生成する
  • 複雑なタンパク質アーキテクチャの設計における ディープラーニングの可能性を探求する.

主な方法:

  • 深いネットワークの幻覚は タンパク質の構造を生成するために使われました
  • 仕様にはプロトメアの数とプロトメアの長さが含まれていた.
  • X線結晶学と冷凍電子顕微鏡を用いた実験的検証.

主要な成果:

  • 設計された7つのタンパク質ホモオリゴーマーが結晶化され,計算モデルと高い構造的類似性を示した (RMSDの中央値:0.6 Å).
  • 3つの巨大なリング構造 (10nm直径) で,最大1550の残留物とC33の対称性は,冷凍-EMで決定された.
  • 生成された構造は,以前に知られているタンパク質構造と著しく異なる.

結論:

  • ディープラーニングにより 多様で新しいタンパク質構造が作られます
  • このアプローチは,複雑なタンパク質ベースのナノマシンとバイオマテリアルの設計の可能性を広げています.