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相关概念视频

Proofreading01:43

Proofreading

Synthesis of new DNA molecules starts when DNA polymerase links nucleotides together in a sequence that is complementary to the template DNA strand. DNA polymerase has a higher affinity for the correct base to ensure fidelity in DNA replication. The DNA polymerase furthermore proofreads during replication, using an exonuclease domain that cuts off incorrect nucleotides from the nascent DNA strand.Errors during Replication Are Corrected by the DNA Polymerase EnzymeGenomic DNA is synthesized in...
Proofreading01:43

Proofreading

Synthesis of new DNA molecules starts when DNA polymerase links nucleotides together in a sequence that is complementary to the template DNA strand. DNA polymerase has a higher affinity for the correct base to ensure fidelity in DNA replication. The DNA polymerase furthermore proofreads during replication, using an exonuclease domain that cuts off incorrect nucleotides from the nascent DNA strand.Errors during Replication Are Corrected by the DNA Polymerase EnzymeGenomic DNA is synthesized in...
Termination of Translation01:44

Termination of Translation

The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
Termination of Translation01:44

Termination of Translation

The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
Proofreading01:31

Proofreading

Synthesis of new DNA molecules is carried out by the enzyme DNA polymerase, which adds nucleotides on the daughter strand complementary to the template DNA strand. DNA polymerase has a higher affinity to add the correct base and ensures fidelity during DNA replication. Furthermore,  it exhibits proofreading activity during replication, using an exonuclease domain that cuts off incorrect nucleotides from the nascent DNA strand.
Errors During Replication are Corrected by the DNA Polymerase Enzyme
Variance01:15

Variance

The deviations show how spread out the data are about the mean. A positive deviation occurs when the data value exceeds the mean, whereas a negative deviation occurs when the data value is less than the mean. If the deviations are added, the sum is always zero. So one cannot simply add the deviations to get the data spread. By squaring the deviations, the numbers are made positive; thus, their sum will also be positive.The standard deviation measures the spread in the same units as the data.

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相关实验视频

Updated: Jul 6, 2026

Molecular Evolution of the Tre Recombinase
12:02

Molecular Evolution of the Tre Recombinase

Published on: May 29, 2008

这就是Erratum Erratum.

D Shapley

    Science (New York, N.Y.)
    |August 26, 1977
    PubMed
    概括

    一个历史纠正将奥斯卡·莫根斯特恩的祖父弗雷德里克三世确定为普鲁士国王和德国皇帝. 他于1888年短暂执政,澄清了之前的错误识别.

    科学领域:

    • 历史准确性 历史准确性
    • 基因谱系 基因谱系 基因谱系
    • 君主制国家君主制国家

    背景情况:

    • 纠正科学出版物中的事实错误对于保持学术诚信至关重要.
    • 准确识别历史人物对于理解家庭和政治背景至关重要.

    研究的目的:

    • 为了纠正对弗雷德里克三世的错误识别,经济学家奥斯卡·莫根斯特恩的祖父.
    • 提供关于弗雷德里克三世的皇室头和统治的准确历史细节.

    主要方法:

    • 对特定问题和引用的页面号码进行审查,用于错误识别.
    • 通过交叉引用历史记录来确认弗雷德里克三世的身份和统治.

    主要成果:

    • 弗雷德里克三世被正确地认定为普鲁士国王和德国皇帝.
    • 他的短暂统治发生在1888年.

    结论:

    • 校正确保在学术话语中准确地代表历史人物.
    • 正确识别弗雷德里克三世澄清了他与奥斯卡·莫根斯特恩的关系以及他的历史意义.

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    Last Updated: Jul 6, 2026

    Molecular Evolution of the Tre Recombinase
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