Proline cis/trans Isomerization in Intrinsically Disordered Proteins and Peptides
Fanni Sebák1, János Szolomájer2, Nándor Papp1,3
1Analytical and BioNMR Laboratory, Institute of Chemistry, Eötvös Loránd University, 1117 Budapest, Hungary.
Frontiers in Bioscience (Landmark Edition)
|July 3, 2023
Summary
Proline cis/trans isomerization in intrinsically disordered proteins (IDPs) affects their function. Neighboring amino acids influence cis-Pro content, which can be measured by NMR spectroscopy.
Area of Science:
- Biochemistry
- Structural Biology
- Protein Science
Background:
- Intrinsically disordered proteins (IDPs) lack stable structures and exist in multiple conformations.
- Proline cis/trans isomerization is a key factor in IDP conformational heterogeneity.
- The cis/trans proline ratio is critical for distinct biological functions.
Purpose of the Study:
- To investigate the influence of neighboring amino acids on cis-Pro isomer formation in IDPs.
- To establish regularities governing cis-Pro content based on amino acid context.
- To utilize NMR spectroscopy for precise cis-Pro content determination.
Main Methods:
- Statistical analysis of experimental literature on proline cis/trans isomerization.
- NMR spectroscopy to quantify cis-Pro content in model peptides and mutated proteins.
- Analysis of amino acid influence within the i ± 4 regions surrounding proline residues.
Main Results:
- The cis-Pro content is significantly influenced by the types of neighboring amino acids.
- Aromatic and positively charged side chains show a notable effect on cis-Pro formation.
- NMR spectral analysis confirmed these dependencies.
Conclusions:
- Understanding neighboring amino acid effects aids in designing protein regions with specific cis-Pro content.
- This research enhances comprehension of IDP roles and functions.
- NMR spectroscopy is vital for characterizing proline isomerization states.
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