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関連する概念動画

Energy Diagrams, Transition States, and Intermediates02:13

Energy Diagrams, Transition States, and Intermediates

Free-energy diagrams, or reaction coordinate diagrams, are graphs showing the energy changes that occur during a chemical reaction. The reaction coordinate represented on the horizontal axis shows how far the reaction has progressed structurally. Positions along the x-axis close to the reactants have structures resembling the reactants, while positions close to the products resemble the products.  Peaks on the energy diagram represent stable structures with measurable lifetimes, while other...
Protein Folding01:22

Protein Folding

Overview
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...
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...
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
Phase Transitions: Melting and Freezing02:39

Phase Transitions: Melting and Freezing

Heating a crystalline solid increases the average energy of its atoms, molecules, or ions, and the solid gets hotter. At some point, the added energy becomes large enough to partially overcome the forces holding the molecules or ions of the solid in their fixed positions, and the solid begins the process of transitioning to the liquid state or melting. At this point, the temperature of the solid stops rising, despite the continual input of heat, and it remains constant until all of the solid is...

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関連する実験動画

Updated: Jun 6, 2026

Measuring Biomolecular DSC Profiles with Thermolabile Ligands to Rapidly Characterize Folding and Binding Interactions
09:15

Measuring Biomolecular DSC Profiles with Thermolabile Ligands to Rapidly Characterize Folding and Binding Interactions

Published on: November 21, 2017

エンドポイント構造からのマクロ分子構成の変化に関連するエネルギー景観.

Arianna Fornili1, Barbara Giabbai, Gianpiero Garau

  • 1Biocrystallography Unit, Division of Immunology, Transplantation, and Infectious Diseases, Scientific Institute San Raffaele, Via Olgettina 58, 20132 Milan, Italy. arianna.fornili@kcl.ac.uk

Journal of the American Chemical Society
|November 19, 2010
PubMed
まとめ

私たちは,タンパク質の形状の変化のエネルギーを定量化するための新しい計算方法を開発しました. このアプローチは,酵素結合を正確に予測し,単一の残留物がどのように作用するかを明らかにします.

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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
07:33

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

関連する実験動画

Last Updated: Jun 6, 2026

Measuring Biomolecular DSC Profiles with Thermolabile Ligands to Rapidly Characterize Folding and Binding Interactions
09:15

Measuring Biomolecular DSC Profiles with Thermolabile Ligands to Rapidly Characterize Folding and Binding Interactions

Published on: November 21, 2017

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
07:33

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

科学分野:

  • バイオケミストリーと構造生物学
  • 計算式生体物理学について

背景:

  • マクロ分子機能は構造の変化によって調節され,リガンド結合と酵素活性に影響を与えます.
  • これらのダイナミックな構造的相互変換のエネルギー学的性質の定量的な特徴付けは,統一された方法が欠如しているため,依然として課題です.

研究 の 目的:

  • 構成的エネルギー景観の定量的な特徴付けのための新しいin silicoアプローチを導入する.
  • ユーザー定義の集団変数なしで複雑な分子再編成の公正な調査を可能にします.

主な方法:

  • 組み合わせた本質的なダイナミクスのサンプリングと不均衡の自由エネルギー計算.
  • バクテリアの核酸ヒドロラゼの構造変化を分析する方法を適用した.

主要な成果:

  • 定量的自由エネルギープロファイルは,酵素の実験的結合定数を正確に予測した.
  • 形状転換の速度を制限する性質を示した.
  • 単一の残留物のプロトネーション状態が基質結合と製品放出における予期せぬ規制的役割を特定した.

結論:

  • この新しい計算アプローチは,マクロ分子構成エネルギー学を研究するための統一された方法を提供します.
  • この技術は,基質結合と製品放出調節を含む酵素機構の洞察を提供します.