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相关概念视频

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 Folding01:22

Protein Folding

Overview
Protein Folding01:22

Protein Folding

Overview
Protein Organization01:13

Protein Organization

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.
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...

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相关实验视频

Updated: May 21, 2026

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

在折聚合物中的核化效应.

Anupam Patgiri1, Stephen T Joy, Paramjit S Arora

  • 1Department of Chemistry, New York University, New York, New York 10003, USA.

Journal of the American Chemical Society
|June 22, 2012
PubMed
概括

β(3) -氨基酸寡合体提供稳定的结构模仿的α-螺旋体. 这些异构的序列显示了与α-螺旋相比的结构刚度增加,受宏循环模板的影响.

科学领域:

  • 生物化学 生物化学
  • 有机化学 有机化学
  • 结构生物学 结构生物学

背景情况:

  • β(3) - 氨基酸和混合α-/β(3) - 残留物的寡合体是α-螺旋体的蛋白质分解稳定的结构模仿物.
  • 这些寡合体甚至可以在短序列中采用定义的构造.

研究的目的:

  • 为了评估与核前螺旋体中的α-氨基酸类似物相比β-3-残留物的影响.
  • 为了研究含有β3残留的异质序列的构造性质.

主要方法:

  • 使用了-交换实验.
  • 对前核螺旋的分析,其α-和β(3)-残留的组成各不相同.

主要成果:

  • 具有"αααβ"重复的异质序列表现出比同质的α-螺旋体更大的形状刚性.
  • 宏观循环的螺旋形状模板显著影响了观察到的刚性.

结论:

  • β(3) 残留物增强了螺旋性寡合体的结构刚性.
  • 宏观循环结构在决定这些阿尔法螺旋模仿的结构稳定性方面发挥着至关重要的作用.

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Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets
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Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets

Published on: November 2, 2011

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
10:50

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets
13:42

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets

Published on: November 2, 2011

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
10:50

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

Published on: September 15, 2010