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Gene Duplication and Divergence02:37

Gene Duplication and Divergence

7.7K
The seminal work of Ohno in 1970 popularized the idea of gene duplication and divergence. DNA sequence comparison studies reveal that a large portion of the genes in bacteria, archaebacteria, and eukaryotes was  generated by gene duplication and divergence, indicating its critical role in evolution.
The duplicated copies of the gene are called Paralogs. Paralogs with similar sequences and functions form a gene family. Across several species, a large number of gene families are...
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Gene Families01:57

Gene Families

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Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
9.7K
Protein Families02:47

Protein Families

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Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key...
16.5K
Hemoglobin01:24

Hemoglobin

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Hemoglobin is a globular protein made up of four subunits. Two of these subunits are alpha chains, and the other two are beta chains. Each subunit contains a molecule of heme, which has an iron atom and can bind to oxygen. When an oxygen molecule binds to one heme group, it changes the shape of hemoglobin, making it easier for the other heme groups to bind oxygen as well.
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...
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Protein and Protein Structure02:15

Protein and Protein Structure

86.0K
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...
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Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

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Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
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関連する実験動画

Updated: Dec 20, 2025

Measurement of Heme Synthesis Levels in Mammalian Cells
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Measurement of Heme Synthesis Levels in Mammalian Cells

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ヘモグロビンの進化における複雑性の起源

Arvind S Pillai1, Shane A Chandler2, Yang Liu3

  • 1Department of Ecology and Evolution, University of Chicago, Chicago, IL, USA.

Nature
|May 29, 2020
PubMed
まとめ
この要約は機械生成です。

現代のヘモグロビンは 古代の単一タンパク質から進化しました 遺伝子の複製と 重要な変異が 複雑な構造と 協力的な酸素結合を 作り出したことを明らかにしました

さらに関連する動画

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis
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T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis

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Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin
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Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

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関連する実験動画

Last Updated: Dec 20, 2025

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Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

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T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis
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科学分野:

  • 進化生物学
  • 分子生物学
  • 生物化学

背景:

  • タンパク質は複合的な構造 (マルチマー) を形成し,協同リガンド結合のような特殊な機能を持つ.
  • これらの複雑なタンパク質の構造と機能の 進化的起源は ほとんど知られていません
  • 脊椎動物のヘモグロビンはテトラマーで 協同結合によって酸素を輸送する.

研究 の 目的:

  • 脊椎動物のヘモグロビンの進化的起源を明らかにする
  • 祖先のタンパク質構造と 進化の中間物質を特定する
  • 複雑なタンパク質の機能の進化を促す 遺伝的・生体学的メカニズムを理解する

主な方法:

  • 祖先のタンパク質の再構築
  • 生物物理的測定法
  • 比較ゲノミクス

主要な成果:

  • 現代ヘモグロビンは 古代のモノマーから進化しました
  • 高酸素親和性を持つ非協力性ホモディマーが重要な進化的中間体として特定された.
  • 2つの特定の変異は,祖先のタンパク質にテトラメリゼーションと協力的な酸素結合を誘導するのに十分であった.
  • 酸素結合とマルチメリゼーションのインターフェースの間の本質的なリンクは,祖先の構造に存在していました.

結論:

  • 複雑なタンパク質の構造と機能は 単純な遺伝的変化によって進化します
  • 進化は,既存の生体物理的特性を再利用して,より高いレベルの分子構造を作り出すことができます.
  • ヘモグロビンの進化は,モノマーから機能的なテトラマーへの段階的なプロセスを示しています.