Jove
Visualize
联系我们
JoVE
x logofacebook logolinkedin logoyoutube logo
关于 JoVE
概览领导团队博客JoVE 帮助中心
作者
出版流程编辑委员会范围与政策同行评审常见问题投稿
图书馆员
用户评价订阅访问资源图书馆顾问委员会常见问题
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experiments存档
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教师资源中心教师网站
使用条款与条件
隐私政策
政策

相关概念视频

Protein Organization01:13

Protein Organization

Overview
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:22

Protein Folding

Overview
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.
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...
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.

您也可能阅读

相关文章

通过共同作者、期刊和引用图与本文相关的文章。

排序
Same author

Spiers Memorial Lecture: Spin-mediated promotion of magnetic metal catalysts.

Faraday discussions·2026
Same author

Fluctuation-Mediated Model for Hydrogen-Inhibited N<sub>2</sub> Dissociation on Iron─Implications for Ambient Ammonia Electrosynthesis.

The journal of physical chemistry letters·2026
Same author

Multi-Objective Catalyst Discovery in High-Entropy Alloy Composition Space: The Role of Noble Metals on the Pareto Front for Oxygen Reduction Reaction.

Angewandte Chemie (International ed. in English)·2026
Same author

The Computational Cation Electrode: A Case Study on CO2RR.

Chemphyschem : a European journal of chemical physics and physical chemistry·2026
Same author

Advanced structural characterization of high-entropy alloy nanostructures: general discussion.

Faraday discussions·2026
Same author

Unraveling the Mixing Entropy-Activity Relationship in High Entropy Alloy Catalysts: The More, The Better?

Journal of the American Chemical Society·2026
Same journal

Switching Site Selectivity in Alkoxyamine Hydration: From Lone-Pair Direction to Solvent Network Dominance.

Journal of the American Chemical Society·2026
Same journal

A Topotactic Leap: 2D Layers to 3D Large-Pore Zeolite.

Journal of the American Chemical Society·2026
Same journal

Enhanced Hydrogen Evolution over Single-Atom Catalysts via Electrostatic Polarization in Contact-electro-catalysis.

Journal of the American Chemical Society·2026
Same journal

Tumor Acidity-Activatable Ionizable Lipid Nanoparticles for Selective Oncolytic Therapy.

Journal of the American Chemical Society·2026
Same journal

Alternating Magnetic Field Promotes Ammonia Cracking by Disrupting the Sabatier Limitation of Ruthenium Catalytic Species.

Journal of the American Chemical Society·2026
Same journal

Bulk Ferromagnetic Icosahedral Quasicrystals without Rapid Quenching.

Journal of the American Chemical Society·2026
查看所有相关文章

相关实验视频

Updated: Jul 7, 2026

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
10:58

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

基于第一原则的Beta-sheet偏好

Jan Rossmeisl1, Iben Kristensen, Misha Gregersen

  • 1Center for Atomic-scale Materials Physics, Technical University of Denmark, DK-2800 Lyngby, Denmark.

Journal of the American Chemical Society
|December 25, 2003
PubMed
概括
此摘要是机器生成的。

氨基酸表现出对蛋白质结构的偏好. 计算分析显示,这些β-sheet倾向与结合能和局部链灵活性相关.

更多相关视频

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

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
08:53

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

Published on: March 21, 2025

相关实验视频

Last Updated: Jul 7, 2026

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
10:58

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

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

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
08:53

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

Published on: March 21, 2025

科学领域:

  • 生物化学 生物化学
  • 计算化学的计算化学
  • 结构生物学 结构生物学

背景情况:

  • 自然氨基酸对特定的二次蛋白质结构表现出明显的偏好.
  • 了解这些偏好对于预测蛋白质折叠和功能至关重要.

研究的目的:

  • 为了研究氨基酸序列和二次结构偏好之间的关系.
  • 通过计算来确定控制β-sheet倾向的因素.

主要方法:

  • 使用密度函数理论 (DFT) 的计算.
  • 在周期模型β表上进行了模拟,该表包含14种不同的氨基酸.
  • 一般化梯度近似 (GGA) 用于电子结构计算.

主要成果:

  • 在统计学确定的β-sheet倾向和计算的结合能之间观察到强烈的相关性.
  • 分析表明,单个多链内的局部灵活性是beta-sheet倾向的关键决定因素.

结论:

  • 这项研究为了解β-sheet形成中的氨基酸偏好提供了计算基础.
  • 局部多的灵活性成为影响二次结构采用的关键因素.