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相关概念视频

Protein Organization01:24

Protein Organization

9.8K
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....
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Protein Folding01:25

Protein Folding

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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...
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Protein Folding01:22

Protein Folding

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Overview
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Conserved Binding Sites01:49

Conserved Binding Sites

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
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Introduction to Actin01:26

Introduction to Actin

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Actin is a highly conserved cytoskeletal protein found abundantly in eukaryotic cells. It constitutes 10% weight of the total cellular protein in muscle cells, while in non-muscle cells, it is lower and makes up around 1–5 percent of the total cell protein. Actin found in the unicellular amoebae and complex multicellular animals is around 80% similar, demonstrating their conservation over a billion years of evolution.  Actin coding genes are conserved within species and across...
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相关实验视频

Updated: Feb 26, 2026

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
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Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

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SimHS-AFMfit-MD:一个综合的方法推断阿尔法-动素原子形态动力学.

Kien Xuan Ngo1,2, Takashi Sumikama1,3,4, Rémi Vuillemot5

  • 1Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kakuma-machi, Kanazawa 920-1192, Japan.

Nano letters
|February 25, 2026
PubMed
概括
此摘要是机器生成的。

本研究介绍了SimHS-AFMfit-MD,这是一种结合高速原子力显微镜 (HS-AFM) 和分子动力学 (MD) 模拟的新方法,以原子分辨率可视化动态蛋白质结构.

关键词:
在AFMfit-MD中.在AFMfit-NMA.阿尔法 - 动因素的作用.在HS-AFMM中.在MD模拟的模拟.没有NMA,没有NMA.在PCA中,PCA是PCA.在 SimHS-AFMfit-MD 中使用.

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A Protocol for Computer-Based Protein Structure and Function Prediction
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相关实验视频

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Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
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科学领域:

  • 生物物理学的生物物理.
  • 结构生物学 结构生物学
  • 计算生物学 计算生物学

背景情况:

  • 像蛋白质这样的灵活分子系统对传统的结构生物学技术提出了挑战.
  • 形状异质性阻碍了详细的原子层次分析.

研究的目的:

  • 在原子分辨率下开发一个整合性框架来推断动态蛋白质构造.
  • 为了可视化实时蛋白质动态,桥梁模拟和成像.

主要方法:

  • 推出了SimHS-AFMfit-MD,将高速原子力显微镜 (HS-AFM) 与分子动力学 (MD) 模拟相结合.
  • 采用基于AFMfit的结构建模,增强非线性正常模式分析 (AFMfit-NMA) 和MD轨迹指导 (AFMfit-MD).
  • 将该方法应用于α-actinin,一种actin交叉链接蛋白.

主要成果:

  • AFMfit-NMA提高了结构的适配精度.
  • AFMfit-MD显著提高了装配性能,与全原子MD模拟保持一致.
  • 从成千上万的HS-AFM图像中生成原子尺度的形状组合.
  • 在α-actinin中揭示了Ca2+依赖的构造转换.

结论:

  • SimHS-AFMfit-MD使蛋白质动态的原子尺度可视化成为可能.
  • 混合方法有效地弥合了计算和实验方法.
  • 这一框架推动了灵活分子系统的研究.