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相关概念视频

Protein Folding01:25

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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.
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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.
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A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
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气相螺旋可以模仿溶液相的行为.

Lindsay J Morrison1, Vicki H Wysocki

  • 1Ohio State University , 484 West 12th Avenue, Columbus, Ohio 43210, United States.

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|September 10, 2014
PubMed
概括
此摘要是机器生成的。

气相的研究表明,在终点的阿尔法螺旋稳定. 分析了双电荷的螺旋形和球形形状,显示了序列和长度的影响稳定性.

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科学领域:

  • 生物物理化学 生物物理化学
  • 质谱测量质量谱测量
  • 蛋白质的构造 蛋白质的构造

背景情况:

  • 溶液中的α螺旋通过终端封闭相互作用来稳定.
  • 气相研究提供了关于内在稳定性质的见解.
  • 之前的溶液阶段研究研究了N端氨基酸效应.

研究的目的:

  • 为了研究气相的螺旋和球形形状.
  • 探索序列和长度对螺旋稳定性的影响.
  • 分析片段的构造偏好.

主要方法:

  • 对气相,双电荷 (XAnK) 的分析.
  • 质谱测量用于研究形状和碎片化.
  • 改变碰撞能量以诱导形状变化.

主要成果:

  • 在气相中观察到的螺旋和球形形状.
  • 螺旋形状的丰度取决于的长度和N端残留物 (X).
  • 螺旋式b离子碎片最好是在较低的碰撞能量下形成的,特别是从螺旋式前体.

结论:

  • 气相研究证实了螺旋稳定在溶液相观察.
  • 碎片稳定性受到长度,N端残留物,前体构造和碰撞能量的影响.
  • 在b-ions.中稳定的螺旋形状需要最小的碎片长度 (b10).