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関連する概念動画

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

19.1K
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...
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Rab Cascades01:25

Rab Cascades

3.2K
Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
3.2K
Rab Proteins01:14

Rab Proteins

4.7K
Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
4.7K
Entropy and Solvation02:05

Entropy and Solvation

7.9K
The process of surrounding a solute with solvent is called solvation. It involves evenly distributing the solute within the solvent. The rule of thumb for determining a solvent for a given compound is that like dissolves like. A good solvent has molecular characteristics similar to those of the compound to be dissolved. For example, polar solutions dissolve polar solutes, and apolar solvents dissolve apolar solutes. A polar solvent is a solvent that has a high dielectric constant (ϵ...
7.9K
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

61.7K
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.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
61.7K
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

18.9K
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関連する実験動画

Updated: Nov 26, 2025

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
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Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors

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ハイドロフォビック・ラッチは 分子複合体を固める

Georg K A Hochberg1, Yang Liu2, Erik G Marklund3

  • 1Department of Ecology and Evolution, University of Chicago, Chicago, IL, USA.

Nature
|December 10, 2020
PubMed
まとめ

多くのタンパク質複合体は"水害性変異性ラチェット"によって持続する. このメカニズムは,多元化が明確な機能上の利点を提供しない場合でも,組み立てられていない形態を不安定にします.

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Single-molecule Manipulation of G-quadruplexes by Magnetic Tweezers
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Single-molecule Manipulation of G-quadruplexes by Magnetic Tweezers

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Nanomanipulation of Single RNA Molecules by Optical Tweezers
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Nanomanipulation of Single RNA Molecules by Optical Tweezers

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関連する実験動画

Last Updated: Nov 26, 2025

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
10:33

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors

Published on: October 26, 2015

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Single-molecule Manipulation of G-quadruplexes by Magnetic Tweezers
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Single-molecule Manipulation of G-quadruplexes by Magnetic Tweezers

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Nanomanipulation of Single RNA Molecules by Optical Tweezers
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科学分野:

  • 分子生物学
  • 進化生物学
  • 構造バイオインフォマティクス

背景:

  • ほとんどのタンパク質は複数のサブユニット複合体として機能する.
  • タンパク質複合体の進化的持続は,マルチメリゼーションの機能的利点の選択にしばしば起因する.
  • しかし,多くの複合体は,その組み立てに起因する既知の機能が欠けている.

研究 の 目的:

  • タンパク質複合体の進化的根絶のための代替メカニズムを調査する.
  • 機能に関係なく 複合体を安定させることができるという仮説を検証する
  • タンパク質の安定性と溶媒の露出が分子構成を維持する役割を探求する.

主な方法:

  • ステロイドホルモン受容体に対する祖先のタンパク質再構成と生化学的測定法.
  • タンパク質のインターフェースと変異傾向の構造バイオインフォマティクス分析.
  • 数百のマルチマーファミリーの データベース分析

主要な成果:

  • ステロイドホルモン受容体内の古くから保存されている水害性インターフェースは,識別可能な機能が欠如しているにもかかわらず,溶媒の曝露時に安定性と集積が低下しているため,根付いています.
  • 普遍的な変異バイアスは,モノマーにおいて有害であるマルチメリックインターフェイス内の埋もれた場所での水害性置換を好みます.
  • 分析されたマルチマー族の大多数は,長期にわたる水害性根絶の証拠を示している.

結論:

  • 分子複合体の固まりを 系統的に駆動する
  • このメカニズムは,多くのタンパク質複合体が機能的に無償で組み合わされている場合でも,その持続性を説明します.
  • タンパク質複合体の安定性は,水性相互作用によって駆動され,進化的持続性における機能的優位性の必要性を覆すことができます.