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Related Concept Videos

From DNA to Protein03:06

From DNA to Protein

The flow of genetic information in cells from DNA to mRNA to protein is described by the central dogma, which states that genes specify the sequence of mRNAs, which in turn specify the sequence of amino acids making up all proteins. The decoding of one molecule to another is performed by specific proteins and RNAs. Because the information stored in DNA is so central to cellular function, it makes intuitive sense that the cell would make mRNA copies of this information for protein synthesis...
Mutations01:39

Mutations

Overview
Mutations01:35

Mutations

Mutations are changes in the sequence of DNA. These changes can occur spontaneously or they can be induced by exposure to environmental factors. Mutations can be characterized in a number of different ways: whether and how they alter the amino acid sequence of the protein, whether they occur over a small or large area of DNA, and whether they occur in somatic cells or germline cells.
Chromosomal Alterations Are Large-Scale Mutations
While point mutations are changes in a single nucleotide in...
Mutations01:39

Mutations

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Improving Translational Accuracy02:07

Improving Translational Accuracy

Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...
Improving Translational Accuracy02:07

Improving Translational Accuracy

Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...

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Related Experiment Video

Updated: May 26, 2026

Removal of an Internal Translational Start Site from mRNA While Retaining Expression of the Full-Length Protein
05:48

Removal of an Internal Translational Start Site from mRNA While Retaining Expression of the Full-Length Protein

Published on: March 16, 2022

A novel coding method for gene mutation correction during protein translation process.

Lei Zhang1, Fengchun Tian, Shiyuan Wang

  • 1College of Communication Engineering, Chongqing University, 174 ShaPingBa District, Chongqing, 400044, PR China. leizhang@cqu.edu.cn

Journal of Theoretical Biology
|December 17, 2011
PubMed
Summary
This summary is machine-generated.

This study introduces a novel method using error-correction coding theory to model and detect translation initiation in prokaryotes. The approach effectively identifies key genetic regions and analyzes mutations, enhancing protein translation efficiency.

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A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes

Published on: May 22, 2018

Area of Science:

  • Molecular Biology
  • Bioinformatics
  • Genetics

Background:

  • Gene mutations can negatively impact protein translation in prokaryotic organisms.
  • Accurate modeling and detection of translation initiation are crucial for understanding gene expression.
  • Existing methods for analyzing mutations in translation initiation sites have limitations.

Purpose of the Study:

  • To propose a novel method for modeling and detecting translation initiation in prokaryotes.
  • To analyze the impact of gene mutations on translation efficiency.
  • To identify biologically significant regions within mRNA leader sequences.

Main Methods:

  • Utilizing error-correction coding theory for modeling translation initiation.
  • Employing a one-dimensional codebook from block coding.
  • Implementing a decoding method based on minimum Hamming distance for efficiency analysis.

Main Results:

  • The proposed method effectively recognizes biologically significant regions like the Shine-Dalgarno sequence.
  • A comprehensive analysis of single and multiple base mutations in Shine-Dalgarno sequences was performed.
  • The method demonstrated robustness against multiple base mutations, unlike some experimental techniques.

Conclusions:

  • The novel error-correction coding-based method accurately models and detects translation initiation in prokaryotes.
  • This approach enhances the understanding and analysis of translation efficiency and genetic regulation.
  • The method offers a robust tool for studying the effects of mutations on gene expression.