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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.

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関連する実験動画

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

D-ガンマ-ヒドロキシバリンを含むポリペプチド鎖.

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
まとめ
この要約は機械生成です。

研究者らは,コーン・スナイルの毒ペプチドに異常なd-アミノ酸,d-Valとd-ガンマ-ヒドロキシヴァリン (d-Hyv) を発見した. これらの発見は,生命の典型的なl-ホモキラリティに異議を唱え,新しい酵素経路を示唆しています.

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

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

Published on: December 19, 2020

関連する実験動画

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

科学分野:

  • バイオケミストリー バイオケミストリー
  • ペプチド化学 ペプチド化学
  • ヴェノム・リサーチ ヴェノム・リサーチとは

背景:

  • 生命は明確なl-ホモキラリティを示し,タンパク質は主にl-アミノ酸を使用しています.
  • コーンスナイルの毒には,様々な生物学的活動を持つ多様なペプチド (コノペプチド) が含まれています.

研究 の 目的:

  • 新しく分離されたコノペプチドにおける異常なアミノ酸の存在と構造的特性を調査する.
  • 新規の構造的モチーフと,それらの合成に関与する潜在的な酵素メカニズムを解明する.

主な方法:

  • 4つのコノペプチド:gld-V/gld-V'とmus-V/mus-V'の分離と浄化について
  • ナノ/ピコ-NMRおよびMS/MS技術を用いた完全なアミノ酸配列の決定.
  • 新しい構造モチーフとその安定化相互作用の分析.

主要な成果:

  • リボソームで発現するポリペプチド鎖の中でd-Valとd-ガンマ-ヒドロキシヴァリン (d-Hyv) の発見.
  • ガンマ-ヒドロキシコノファンの新しいSer-d-Hyv-Trpモチーフの特定,特定の相互作用によって安定化.
  • 典型的な制約が欠如し,高ヒドロキシル化を示す非典型コノファンおよびガンマ-ヒドロキシコノファンの特徴.

結論:

  • コノペプチドに含まれるd-アミノ酸の存在は,生物学的ホモキラリティの基本原理に異議を唱える.
  • 新しい構造的モチーフとコーン・スナイルの毒の潜在的ハイパーヒドロキシル化メカニズムは,神経のターゲティングを強化する.
  • この発見は,d-Val酸化に関与するd-ステレオ固有の酵素の存在を示唆しています.