Related Experiment Video
Updated: Jan 27, 2026
09:37
Preparation of Fungal and Plant Materials for Structural Elucidation Using Dynamic Nuclear Polarization Solid-State NMR
Published on: February 12, 2019
7.9K
Elucidating ligand-bound structures of membrane proteins using solid-state NMR spectroscopy.
1Department of Chemistry, Massachusetts Institute of Technology, 170 Albany Street, Cambridge, MA 02139, United States.
Current Opinion in Structural Biology
|March 24, 2019
Summary
Magic-angle-spinning solid-state NMR spectroscopy reveals protein-ligand interactions in lipid membranes. This review highlights recent studies on membrane proteins, cholesterol, lipids, and peptides for biological insights.
Area of Science:
- Biophysics
- Structural Biology
- Biochemistry
Background:
- Magic-angle-spinning (MAS) solid-state NMR spectroscopy is a powerful technique for studying biomolecular structures and interactions.
- Understanding protein-ligand interactions within lipid membranes is crucial for various biological processes.
Purpose of the Study:
- To review recent advances in solid-state NMR applications for investigating protein-ligand interactions in lipid membranes.
- To highlight the insights gained into biological mechanisms through these studies.
Main Methods:
- Utilizing MAS solid-state NMR spectroscopy in synthetic or native lipid bilayers.
- Employing multinuclear detection for comprehensive structural information.
- Applying distance measurements to map ligand-binding sites.
- Leveraging dynamic nuclear polarization and 1H detection for enhanced sensitivity.
Main Results:
- Detailed structural information on protein-ligand complexes in membrane environments.
- Identification of specific binding sites for cholesterol, lipids, substrates, and peptides.
- Insights into the dynamics and mechanisms of membrane protein function.
Conclusions:
- Solid-state NMR is a versatile tool for elucidating functionally important protein-ligand interactions in lipid membranes.
- These studies provide critical insights into viral processes, transmembrane signaling, and substrate transport.
More Related Videos
Related Concept Videos
02:22Structures of Solids
17.6K
Solids in which the atoms, ions, or molecules are arranged in a definite repeating pattern are known as crystalline solids. Metals and ionic compounds typically form ordered, crystalline solids. A crystalline solid has a precise melting temperature because each atom or molecule of the same type is held in place with the same forces or energy. Amorphous solids or non-crystalline solids (or, sometimes, glasses) which lack an ordered internal structure and are randomly arranged. Substances that...
17.6K
01:19NMR Spectroscopy Of Amines
11.1K
In proton NMR spectroscopy, primary amines and secondary amines showcase their N–H protons as a broad signal in the chemical shift range between δ 0.5 and 5 ppm. The exact position in this range depends on several factors, including sample concentration, hydrogen bonding, and the type of solvent used. Since amine protons undergo fast proton exchange in solution, the protons are labile and therefore do not participate in any splitting with adjacent protons. Thus, the observed peak is...
11.1K
01:16Introduction to Membrane Proteins
80.9K
The cell membrane, or plasma membrane, is an ever-changing landscape. It is described as a fluid mosaic where various macromolecules are embedded in the phospholipid bilayer. Among the macromolecules are proteins. The protein content varies across cell types. For example, mitochondrial inner membranes contain ~76% protein content, while myelin contains ~18% protein content. Individual cells contain many types of membrane proteins—red blood cells contain over 50—and different cell...
80.9K
02:15Protein and Protein Structure
87.2K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
A protein's shape is critical to its function. For example, an enzyme...
87.2K
01:14NMR Spectroscopy of Aromatic Compounds
6.3K
Aromatic compounds can be identified or analyzed using proton NMR and carbon‐13 NMR. Typically, aromatic hydrogens or hydrogens directly bonded to the aromatic rings are strongly deshielded by the aromatic ring current. Therefore, they absorb in the range of 6.5–8.0 ppm in proton NMR spectra. For instance, aromatic hydrogens directly bonded to the benzene ring absorb at 7.3 ppm. However, aromatic hydrogens of larger rings absorb farther upfield or downfield than the ideal range.
6.3K
01:34NMR Spectroscopy of Benzene Derivatives
11.1K
Simple unsubstituted benzene has six aromatic protons, all chemically equivalent. Therefore, benzene exhibits only a singlet peak at δ 7.3 ppm in the 1H NMR spectrum. The observed shift is far downfield because the aromatic ring current strongly deshields the protons. Any substitution on the benzene ring makes the aromatic protons nonequivalent, and the protons split each other. The peak is, therefore, no longer a singlet and the splitting pattern and their associated coupling...
11.1K