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Updated: Jul 19, 2026

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
Published on: December 27, 2016
Protein N-terminal modifications: molecular machineries and biological implications
Hanne Øye1, Malin Lundekvam1, Alessia Caiella1
1Department of Biomedicine, University of Bergen, Bergen, Norway.
Eukaryotic proteins undergo N-terminal (Nt) modifications by enzymes, impacting protein function and biological processes. This review covers Nt modifications, their enzymes, and their roles in health and disease.
Area of Science:
- Biochemistry
- Molecular Biology
- Proteomics
Background:
- Most eukaryotic proteins are modified at their N-terminus (Nt).
- These modifications are enzyme-mediated and sequence-dependent.
- Nt modifications are crucial for regulating protein function and cellular processes.
Purpose of the Study:
- To provide an overview of protein N-terminal modifications.
- To discuss the enzymes involved in Nt modifications.
- To highlight the biological impact and disease relevance of Nt modifications.
Main Methods:
- Literature review of N-terminal modification enzymes.
- Analysis of co- and post-translational modification mechanisms.
- Compilation of biological roles and disease associations.
Main Results:
- Identified diverse Nt modifications including acetylation, methylation, and oxidation.
- Cataloged enzymes such as peptidases, transferases, oxygenases, and ligases.
- Demonstrated Nt modifications' roles in protein targeting, stability, and complex formation.
Conclusions:
- N-terminal modifications are fundamental to proteome complexity and biological regulation.
- Dysregulation of Nt-modifying enzymes is linked to human diseases.
- Understanding Nt modifications is vital for comprehending cellular functions and disease mechanisms.
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