Probing Noncovalent Interactions by Fast Magic-Angle Spinning NMR at 100 kHz and More

Area of Science:

• Chemical Physics
• Biophysical Chemistry
• Spectroscopy

Background:

• Noncovalent interactions are fundamental to molecular recognition in chemistry and biology.
• Processes include supramolecular chemistry, catalysis, protein folding, and biomolecular binding.
• Understanding these interactions in solids is crucial for various scientific disciplines.

Purpose of the Study:

• To review recent advancements in probing noncovalent interactions using proton-detected solid-state Nuclear Magnetic Resonance (NMR) spectroscopy.
• To highlight the impact of high-frequency Magic-Angle Spinning (MAS) and high magnetic fields on NMR capabilities.
• To showcase applications in diverse systems, from protein-nucleic acid complexes to small molecule interactions.

Main Methods:

• Utilizing proton-detected solid-state Nuclear Magnetic Resonance (NMR) spectroscopy.
• Employing Magic-Angle Spinning (MAS) at frequencies of 100 kHz and above.
• Leveraging high static magnetic field strengths up to 28.2 T (1200 MHz proton Larmor frequency).

Main Results:

• Improved resolution and sensitivity in proton-detected solid-state NMR achieved through technological advancements.
• Demonstrated ability to study complex systems, including large motor proteins and calixarene-lanthanide complexes.
• Successful characterization of noncovalent interactions like protein-nucleic acid binding and hydrogen-π interactions in solid states.

Conclusions:

• Proton-detected solid-state NMR, particularly at high MAS frequencies and fields, is a powerful technique for investigating noncovalent interactions.
• These advancements provide fundamental insights into molecular recognition processes in various chemical and biological systems.
• The reviewed developments enable detailed studies of complex solid-state systems previously inaccessible.