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Proline Ring-Inversion Dynamics in Peptides Enable Cross-Relaxation-Based Dynamic Nuclear Polarization
Florian Taube1, Max Gierth1, Georg Künze2,3,4
1Institute of Chemistry and Department Life, Light & Matter, University Rostock, Rostock, Germany.
Specific cross-relaxation enhancement by active motions under DNP (SCREAM-DNP) was investigated in proline-containing peptides. Local structure significantly impacts proline dynamics and SCREAM-DNP efficiency, offering insights for structural biology applications.
Area of Science:
- Biophysical Chemistry
- Structural Biology
- Nuclear Magnetic Resonance Spectroscopy
Background:
- Dynamic nuclear polarization (DNP) uniformly enhances Nuclear Magnetic Resonance (NMR) signals.
- Site-specific enhancement is crucial for analyzing large biomolecules.
- Specific cross-relaxation enhancement by active motions under DNP (SCREAM-DNP) leverages molecular dynamics for targeted signal amplification.
Purpose of the Study:
- To investigate the impact of local structural context on proline dynamics and SCREAM-DNP efficiency.
- To understand how proline's incorporation into peptides affects its conformational dynamics under DNP conditions.
- To identify structural motifs that modulate site-specific DNP enhancement in proline-containing systems.
Main Methods:
- Systematic investigation of SCREAM-DNP in proline and proline-containing derivatives.
- Comparative analysis of proline in different sequence positions within dipeptides.
- Energy barrier calculations to support experimental findings and provide mechanistic insights.
Main Results:
- SCREAM-DNP efficiency is modulated by the local structural context of proline within peptides.
- Specific structural motifs were identified as influencing the dynamics relevant to SCREAM-DNP.
- Experimental observations were corroborated by computational energy barrier calculations.
Conclusions:
- Proline's conformational dynamics, crucial for SCREAM-DNP, are sensitive to its sequence context in peptides.
- Understanding these dynamics provides mechanistic insight into site-specific DNP.
- This work guides the application of SCREAM-DNP for structural biology studies of proline-containing biomolecules.
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