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Related Concept Videos

Nucleotide Excision Repair01:38

Nucleotide Excision Repair

DNA Distortion and Damage
Cells are regularly exposed to mutagens—factors in the environment that can damage DNA and generate mutations. UV radiation is one of the most common mutagens and is estimated to introduce a significant number of changes in DNA. These include bends or kinks in the structure, which can block DNA replication or transcription. If these errors are not fixed, the damage can cause mutations, which in turn can result in cancer or disease depending on which sequences are...
Nucleotide Excision Repair01:08

Nucleotide Excision Repair

Overview
Overview of DNA Repair02:25

Overview of DNA Repair

In order to be passed through generations, genomic DNA must be undamaged and error-free. However, every day, DNA in a cell undergoes several thousand to a million damaging events by natural causes and external factors. Ionizing radiation such as UV rays, free radicals produced during cellular respiration, and hydrolytic damage from metabolic reactions can alter the structure of DNA. Damages caused include single-base alteration, base dimerization, chain breaks, and cross-linkage.
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Proteins: From Genes to Degradation

Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA molecules by RNA...
Proteins: From Genes to Degradation02:11

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Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA molecules by RNA...
Protein Denaturation01:28

Protein Denaturation

The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...

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Genetically encoding protein oxidative damage.

Heinz Neumann1, Jennifer L Hazen, John Weinstein

  • 1Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, United Kingdom.

Journal of the American Chemical Society
|March 7, 2008
PubMed
Summary
This summary is machine-generated.

Researchers developed a method to precisely insert 3-nitrotyrosine (3-NT) into proteins, aiding disease research. This technique allows studying the impact of 3-NT on protein function in conditions like Alzheimer's and Parkinson's disease.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Engineering

Background:

  • Posttranslational modification producing 3-nitrotyrosine (3-NT) is linked to over 50 diseases, including neurodegenerative disorders and cancer.
  • Elevated 3-NT levels in aging tissues predict disease risk, highlighting the need to study its functional impact.

Purpose of the Study:

  • To engineer an aminoacyl-tRNA synthetase/tRNA pair for site-specific, cotranslational incorporation of 3-NT into proteins.
  • To demonstrate the utility of this system for investigating how specific 3-NT modifications affect protein function in disease models.

Main Methods:

  • Evolution and characterization of a novel aminoacyl-tRNA synthetase/tRNA pair.
  • Site-specific incorporation of 3-NT into proteins during translation.
  • Preparation of homogeneously nitrated manganese superoxide dismutase (MnSOD) at a disease-relevant site.

Main Results:

  • Successful development of a system for genetically encoded, site-specific 3-NT incorporation.
  • Demonstration of the system's utility by producing homogeneously 3-NT-modified MnSOD.
  • Analysis of the functional consequences of site-specific nitration on MnSOD activity.

Conclusions:

  • The engineered aminoacyl-tRNA synthetase/tRNA pair enables precise control over protein nitration.
  • This method provides a powerful tool for studying the role of 3-NT in various disease states.
  • Facilitates research into protein function alterations in neurological disorders, inflammation, and aging.