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相关概念视频

Protein Organization01:13

Protein Organization

Overview
Protein Folding01:22

Protein Folding

Overview
Amino acids03:42

Amino acids

Amino acids are the monomers that comprise proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom, or the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. Every amino acid also has another atom or group of atoms bonded to the central atom known as the R group. There are 20 common amino acids present in proteins, each with a different R group. Variation in the amino acid sequence is responsible for...
Peptide Bonds02:43

Peptide Bonds

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...
Protein and Protein Structure02:15

Protein and Protein Structure

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 can...
Basicity of Aliphatic Amines01:21

Basicity of Aliphatic Amines

Amines can behave as Brønsted–Lowry bases by accepting a proton from the acid to form corresponding conjugate acids. Due to a lone pair of nonbonding electrons, aliphatic amines can also act as Lewis bases by forming a covalent bond with an electrophile.
To measure the basicity of amines, two conventions are generally used. The first defines Kb as the basicity constant for the deprotonation reaction of water by the amine, as presented in Figure 1. Conventionally, lower Kb indicates higher...

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相关实验视频

Updated: Jul 13, 2026

Determination of the Gas-phase Acidities of Oligopeptides
11:00

Determination of the Gas-phase Acidities of Oligopeptides

Published on: June 24, 2013

在短的氨酸上吸附水分子:最短的气相氨酸基螺旋体有多短?

Motoya Kohtani1, Martin F Jarrold

  • 1Chemistry Department, Indiana University, 800 East Kirkwood Avenue, Bloomington, Indiana 47405, USA.

Journal of the American Chemical Society
|July 9, 2004
PubMed
概括

水吸附显示出不同的结构. 氨酸 (Ac-A(n) K+H(+)) 在n=8左右过渡到螺旋形状,显示水吸附率降低,与球形不同.

科学领域:

  • 化学物理 化学物理
  • 生物物理化学 生物物理化学
  • 频谱学是一种光谱学方法.

背景情况:

  • 体构造会影响与水的相互作用.
  • 之前的研究已经确定了氨酸中的螺旋和球状状态.
  • 在这些形状之间,水吸附强度大大不同.

研究的目的:

  • 为了研究未溶解的Ac-A(n) K+H(+) 和Ac-KA(n) +H(+) 中的水吸附.
  • 为了确定氨酸,氨酸和氨酸的构造过渡点.
  • 为了将水吸附倾向与气相中的二次结构相关联.

主要方法:

  • 平衡水吸附度测量. 在平衡水吸附度测量.
  • 质谱法用于分析-水复合体.
  • 对于氨酸,氨酸和氨酸的链长度不同 (n=4-10).

主要成果:

  • Ac-KA(n) +H(+) (球状) 显示出强烈的吸水能力.
  • Ac-A(n) K+H(+) 对n<8.8强烈吸附水.
  • 在n=8-10时,Ac-A(n) K+H(+) 的水吸附率显著下降表明螺旋转变.

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Preparation of Mechanically Stable Self-Assembled Peptides Hydrogels

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相关实验视频

Last Updated: Jul 13, 2026

Determination of the Gas-phase Acidities of Oligopeptides
11:00

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Published on: June 24, 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

Preparation of Mechanically Stable Self-Assembled Peptides Hydrogels
05:24

Preparation of Mechanically Stable Self-Assembled Peptides Hydrogels

Published on: September 6, 2024

结论:

  • 在n=8.8时,螺旋结构出现在Ac-A(n) K+H(+) 中.
  • 在n=8时,Ac-V(n) K+H(+) 和Ac-L(n) K+H(+) 的螺旋形成也被建议.
  • 水吸附是一种敏感的探针,用于气相形状.