Sample interview questions: Can you discuss your familiarity with protein post-translational modifications and their analysis?
Sample answer:
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Protein phosphorylation:
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A common post-translational modification involving the addition of a phosphate group to a serine, threonine, or tyrosine residue.
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Typically analyzed using techniques such as immunoblotting, mass spectrometry, or phosphoproteomics.
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Glycosylation:
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The attachment of a sugar molecule to a protein.
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Can be analyzed using techniques such as lectin blotting, mass spectrometry, or glycomics.
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Ubiquitination:
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The attachment of a ubiquitin molecule to a protein, often targeting it for degradation.
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Can be analyzed using techniques such as immunoblotting, mass spectrometry, or ubiquitinomics.
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Acetylation:
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The addition of an acetyl group to a lysine residue.
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Can be analyzed using techniques such as immunoblotting, mass spectrometry, or acetylomics.
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Methylation:
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The addition of a methyl group to a lysine or arginine residue.
- Can be analyzed using techniques such as immunoblotting, mass spectrometry, or methylomics.
In addition to these common modifications, there are many other types of post-translational modifications that can occur.
Analysis of Protein Post-Translational Modifications:
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Mass spectrometry:
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A powerful technique for identifying and quantifying post-translational modifications.
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Can be used to analyze a wide variety of modifications, including phosphorylation, glycosylation, ubiquitination, acetylation, and methylatio… Read full answer
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