Jove
Visualize
联系我们
JoVE
x logofacebook logolinkedin logoyoutube logo
关于 JoVE
概览领导团队博客JoVE 帮助中心
作者
出版流程编辑委员会范围与政策同行评审常见问题投稿
图书馆员
用户评价订阅访问资源图书馆顾问委员会常见问题
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experiments存档
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教师资源中心教师网站
使用条款与条件
隐私政策
政策

相关概念视频

What are Proteins?01:55

What are Proteins?

Overview
Protein Organization01:13

Protein Organization

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...
What are Proteins?01:28

What are Proteins?

Proteins are polymers of amino acids linked together by peptide bonds. Proteins and polypeptides are interchangeably used to refer to long chains of amino acids. However, polypeptides have a molecular weight of fewer than 10,000 daltons, while proteins have greater molecular weight.  Polypeptides with less than 20 amino acids are called oligopeptides or simply peptides. Interactions among the constituent amino acid side chains of proteins help them fold into a stable 3-dimensional structure...
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.

您也可能阅读

相关文章

通过共同作者、期刊和引用图与本文相关的文章。

排序
Same author

Matrix metalloproteinase 13 (MMP-13) processing of type II collagen is altered by antibodies and citrullination found in the early stages of rheumatoid arthritis.

Matrix biology : journal of the International Society for Matrix Biology·2025
Same author

Pharmacogenomic Drug-Gene Interactions in Geriatric Emergency Department Patients Who Sustained Falls: A Pilot Study.

The western journal of emergency medicine·2025
Same author

Membrane-Type 5 Matrix Metalloproteinase (MT5-MMP): Background and Proposed Roles in Normal Physiology and Disease.

Biomolecules·2025
Same author

Effects of a nationwide teledermatology program on access to care for skin cancer and premalignant lesions in public and private health care: A retrospective case-control analysis of data from eight Spanish hospitals.

Journal of the American Academy of Dermatology·2025
Same author

Large-scale elimination of subterranean termite colonies of the genus Reticulitermes (Blattodea: Heterotermitidae) from town centers in Spain.

Journal of economic entomology·2025
Same author

Novel Insights into the Catalytic Mechanism of Collagenolysis by Zn(II)-Dependent Matrix Metalloproteinase-1.

Biochemistry·2024

相关实验视频

Updated: Jul 10, 2026

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope
08:09

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

Published on: March 24, 2017

含有D--基瓦林的多链.

Katarzyna Pisarewicz1, David Mora, Fred C Pflueger

  • 1Department of Chemistry & Biochemistry and Center of Excellence in Biomedical & Marine Biotechnology, Florida Atlantic University, 777 Glades Road, Boca Raton, Florida 33431, USA.

Journal of the American Chemical Society
|April 28, 2005
PubMed
概括
此摘要是机器生成的。

研究人员在牛毒中发现了不寻常的d-氨基酸,d-Val和d-gamma-hydroxyvaline (d-Hyv). 这些发现挑战了生命的典型l-同质性,并提出了新的酶途径.

更多相关视频

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides
09:54

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Published on: August 20, 2018

Homogeneous Glycoconjugate Produced by Combined Unnatural Amino Acid Incorporation and Click-Chemistry for Vaccine Purposes
13:53

Homogeneous Glycoconjugate Produced by Combined Unnatural Amino Acid Incorporation and Click-Chemistry for Vaccine Purposes

Published on: December 19, 2020

相关实验视频

Last Updated: Jul 10, 2026

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope
08:09

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

Published on: March 24, 2017

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides
09:54

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Published on: August 20, 2018

Homogeneous Glycoconjugate Produced by Combined Unnatural Amino Acid Incorporation and Click-Chemistry for Vaccine Purposes
13:53

Homogeneous Glycoconjugate Produced by Combined Unnatural Amino Acid Incorporation and Click-Chemistry for Vaccine Purposes

Published on: December 19, 2020

科学领域:

  • 生物化学 生物化学
  • 类化学 类化学
  • 毒药研究 毒药研究

背景情况:

  • 生命表现出明显的l-homochirality,蛋白质主要使用l-氨基酸.
  • 螺的毒液含有多种不同的 (conopeptides),具有不同的生物活动.

研究的目的:

  • 调查新分离的类中异常氨基酸的存在和结构特征.
  • 阐明它们的合成中涉及的新型结构动机和潜在的酶机制.

主要方法:

  • 分离和净化四种共:gld-V/gld-V'和mus-V/mus-V'.
  • 使用纳米/皮科-NMR和MS/MS技术确定完整的氨基酸序列.
  • 分析新型结构图案及其稳定相互作用.

主要成果:

  • 在核糖体表达的多链中发现d-Val和d-gamma-hydroxyvaline (d-Hyv).
  • 鉴定了一种新的Ser-d-Hyv-Trp基因在玛-基可诺芬中,通过特定的相互作用稳定.
  • 非典型的可诺芬和玛-基可诺芬缺乏典型的约束,并表现出高基化.

结论:

  • 在可诺酸中存在d-氨基酸,这挑战了生物同化性基本原理.
  • 牛毒中的新型结构图案和潜在的过氧化机制增强了神经元的向.
  • 这些发现表明,d-val氧化过程中存在d-stereospecific酶.