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Updated: Jun 12, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

A resonance assignment method for oriented-sample solid-state NMR of proteins.

Robert W Knox¹, George J Lu, Stanley J Opella

¹Department of Chemistry, North Carolina State University, 2620 Yarbrough Drive, Raleigh, North Carolina 27695-8204, USA.

Journal of the American Chemical Society

|June 1, 2010

Summary

This summary is machine-generated.

This study introduces a new method for assigning solid-state NMR spectra of uniformly nitrogen-15 labeled membrane proteins. The technique confirms existing assignments and aids in determining protein structures without specialized labeling.

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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

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Published on: September 17, 2017

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D ¹H NMR

Published on: December 16, 2013

Area of Science:

Structural Biology
Biophysics
Nuclear Magnetic Resonance (NMR) Spectroscopy

Background:

Assigning solid-state NMR spectra of membrane proteins is crucial for structure determination.
Uniaxially aligned proteins offer unique insights but pose assignment challenges.
Existing methods often require selectively labeled samples, limiting broad applicability.

Purpose of the Study:

To propose a general sequential assignment strategy for uniformly (15)N-labeled uniaxially aligned membrane proteins.
To demonstrate the method's efficacy using magnetically aligned Pf1 phage coat protein.
To facilitate the structure determination of membrane proteins via solid-state NMR.

Main Methods:

Employing mismatched Hartmann-Hahn magnetization transfer for proton-mediated correlations between (15)N backbone spins.
Acquiring and overlaying exchanged and nonexchanged separated local field spectra.
Utilizing uniaxially aligned membrane proteins, specifically Pf1 phage coat protein.

Main Results:

Successful confirmation of most original assignments from literature without requiring selectively labeled samples.
Distinguishing cross-peaks from main peaks by comparing different spectral acquisitions.
Demonstrated applicability to proteins of arbitrary topology.

Conclusions:

The proposed sequential assignment strategy is effective for uniformly (15)N-labeled uniaxially aligned membrane proteins.
This method simplifies spectral assignment, reducing the need for complex labeling strategies.
The technique is valuable for future solid-state NMR-based structure determination of membrane proteins.