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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.

Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry
|June 14, 2026
PubMed
Summary
This summary is machine-generated.

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.

Keywords:
SCREAM‐DNPamino acidsprolinepuckering dynamics

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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.