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Membrane Proteins Structure and Dynamics by Nuclear Magnetic Resonance

Sergey Maltsev, Gary A. Lorigan

10.1002/cphy.c110022

Source: Volume 1, Issue 4, October 2011

Published online: October 2011

Full Article on Wiley Online Library



Abstract

Membrane proteins represent a challenging class of biological systems to study. They are extremely difficult to crystallize and in most cases they retain their structure and functions only in membrane environments. Therefore, commonly used diffraction methods fail to give detailed molecular structure and other approaches have to be utilized to obtain biologically relevant information. Nuclear magnetic resonance (NMR) spectroscopy, however, can provide powerful structural and dynamical constraints on these complicated systems. Solution‐ and solid‐state NMR are powerful methods for investigating membrane proteins studies. In this work, we briefly review both solution and solid‐state NMR techniques for membrane protein studies and illustrate the applications of these methods to elucidate proteins structure, conformation, topology, dynamics, and function. Recent advances in electronics, biological sample preparation, and spectral processing provided opportunities for complex biological systems, such as membrane proteins inside lipid vesicles, to be studied faster and with outstanding quality. New analysis methods therefore have emerged, that benefit from the combination of sample preparation and corresponding specific high‐end NMR techniques, which give access to more structural and dynamic information. © 2011 American Physiological Society. Compr Physiol 1:2175‐2187, 2011.

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Figure 1. Figure 1.

Different types and organizations of proteins in lipid bilayer.
Figure 2. Figure 2.

Micelle, bicelle, and bilayer models.
Figure 3. Figure 3.

SDS, DPC, and DHPC structures.
Figure 4. Figure 4.

(A) A MAS rotor in a magnetic field. (B) Typical line shapes for static sample (left) and rotated fast around the magic angle (right).
Figure 5. Figure 5.

(A) A MAS rotor in a magnetic field. (B) Typical line shapes for static sample (left) and rotated fast around the magic angle (right).
Figure 6. Figure 6.

A schematic representation of a PISA wheel pattern. The circles correspond to 15N signals from different residues of the α‐helix.
Figure 7. Figure 7.

DAGK trimer.


Figure 1.

Different types and organizations of proteins in lipid bilayer.



Figure 2.

Micelle, bicelle, and bilayer models.



Figure 3.

SDS, DPC, and DHPC structures.



Figure 4.

(A) A MAS rotor in a magnetic field. (B) Typical line shapes for static sample (left) and rotated fast around the magic angle (right).



Figure 5.

(A) A MAS rotor in a magnetic field. (B) Typical line shapes for static sample (left) and rotated fast around the magic angle (right).



Figure 6.

A schematic representation of a PISA wheel pattern. The circles correspond to 15N signals from different residues of the α‐helix.



Figure 7.

DAGK trimer.

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Article Title: Membrane Proteins Structure and Dynamics by Nuclear Magnetic Resonance
 

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Sergey Maltsev, Gary A. Lorigan. Membrane Proteins Structure and Dynamics by Nuclear Magnetic Resonance. Compr Physiol 2011, 1: 2175-2187. doi: 10.1002/cphy.c110022