Examples of Posttranslational modification in the following topics:
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- Posttranslational modification (PTM) is the chemical modification of a protein after its translation.
- After translation, the posttranslational modification of amino acids extends the range of functions of the protein by attaching it to other biochemical functional groups (such as acetate, phosphate, various lipids, and carbohydrates), changing the chemical nature of an amino acid (e.g., citrullination), or making structural changes (e.g., formation of disulfide bridges).
- This amino acid is usually taken off during post-translational modification.
- Non-standard amino acids that are found in proteins are formed by post-translational modification, which is modification after translation during protein synthesis.
- Such modifications can also determine the localization of the protein.
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- Vitamin K is a group of structurally similar, fat-soluble vitamins that are needed for the posttranslational modification of certain proteins required for blood coagulation and in metabolic pathways in bone and other tissue .
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- In one, the modified nucleotide cannot be recognized by the polymerase or reverse transcriptase; in such cases, the chain ends at the site of modification.
- In the other, the modification is converted in a later step of the analysis to a strand break by chemical treatment.
- For instance, the sites of modifications by dimethyl sulfate (DMS) can be identified by treating DNA with DMS, exposing the sample to conditions that break the backbone at the site of modification, followed by primer extension.
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- Second, as mentioned above many proteins experience post-translational modifications that profoundly affect their activities.
- Third, many transcripts give rise to more than one protein through alternative splicing or alternative post-translational modifications.
- One way in which a particular protein can be studied is to develop an antibody which is specific to that modification.
- There are also antibodies specific to other modifications.
- These can be used to determine the set of proteins that have undergone the modification of interest.
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- Other human proteins that are used as drugs require biological modifications that only the cells of mammals, such as cows, goats, and sheep, can provide.
- Genetic modifications introduced to a protein have many advantages over chemical modifications.
- Bacteria did not develop sophisticated mechanisms for performing post-translational modifications that are present in higher organisms.
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- Non-standard amino acids that are found in proteins are formed by post-translational modification, which is modification after translation during protein synthesis.
- These modifications are often essential for the function or regulation of a protein.
- Another example is the formation of hypusine in the translation initiation factor EIF5A, through modification of a lysine residue.
- Such modifications can also determine the localization of the protein, e.g., the addition of long hydrophobic groups can cause a protein to bind to a phospholipid membrane.
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- Whole-genome DNA-binding analysis is a powerful tool for analyzing epigenetic modifications and DNA sequences bound to regulatory proteins.
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- Protein tags are also useful for specific enzymatic modification (such as biotin ligase tags) and chemical modification (FlAsH) tag.
- Often tags are combined to produce multifunctional modifications of the protein.
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- With advances in medicinal chemistry, most of today's antibacterials chemically are semisynthetic modifications of various natural compounds.
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- Post-transcriptional modification is simpler than in eukaryotes, since most archaean genes lack introns, although there are many introns in their transfer RNA and ribosomal RNA genes, and introns may occur in a few protein-encoding genes.