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相关概念视频

Protein and Protein Structure02:15

Protein and Protein Structure

79.8K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
79.8K
Protein Folding01:22

Protein Folding

118.5K
Overview
118.5K
Protein Organization01:24

Protein Organization

6.6K
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....
6.6K
Protein Denaturation01:28

Protein Denaturation

4.3K
The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
4.3K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

3.8K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
3.8K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

10.9K
Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
10.9K

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相关实验视频

Updated: Jul 23, 2025

A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

68.7K

总体蛋白质结构质量评估使用键参数.

Pavel V Afonine1, Oleg V Sobolev1, Nigel W Moriarty1

  • 1Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.

Acta crystallographica. Section D, Structural biology
|July 11, 2023
PubMed
概括

精制低分辨率的原子模型是很困难的. 新的方法使用键几何学,蛋白质中保存的特征,以验证原子模型,提高准确性而不损害现有的验证工具.

关键词:
原子模型的改进 原子模型的改进低温电磁波冷却器 (Cryo-EM) 是一个非常好的方法.结晶学 结晶学是指结晶学.通过键形成键.验证验证的时间

更多相关视频

Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures
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Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures

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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

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相关实验视频

Last Updated: Jul 23, 2025

A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

68.7K
Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures
10:10

Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures

Published on: December 1, 2020

5.0K
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

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科学领域:

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

背景情况:

  • 由于实验数据细节不足,低分辨率的原子模型精细化存在挑战.
  • 当前的精制实践经常使用Ramachandran图片和rotameric状态,可能会降低它们的验证能力.
  • 需要新的模型验证标准,这些标准通常不会被用作改进目标.

研究的目的:

  • 调查键几何学的实用性,作为原子模型验证的新标准.
  • 建立一种使用保存键分布评估原子模型质量的方法.

主要方法:

  • 从蛋白质数据库中对高分辨率蛋白质模型中的键几何学的系统分析.
  • 的供与接受原子分布及其几何性质的表征.
  • 基于观察到的键几何图案的验证方法的开发.

主要成果:

  • 分析显示了质量过的蛋白质结构中键的明显和保存的几何分布.
  • 这些保存的几何特征可以量化并用于评估原子模型质量.
  • 拟议的方法为原子模型提供了一个独立的验证标准.

结论:

  • 键几何学为原子模型验证提供了一种有价值且未得到充分利用的资源,特别是在低分辨率下.
  • 这种方法提高了原子模型的可靠性,而不干扰现有的验证指标.
  • 这些发现有助于更准确地确定和分析蛋白质结构.