Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Chemical Shift: Internal References and Solvent Effects

Chemical Shift: Internal References and Solvent Effects

In an NMR sample, precise measurement of the absolute absorption frequencies of nuclei is difficult. A standard internal reference compound is added, and the frequency difference between the reference signal and sample signals is measured.
The internal reference compound generally used in NMR spectroscopy is tetramethylsilane (TMS). TMS is preferred because it is chemically inert, soluble in NMR solvents, and easily removable. Also, the highly shielded methyl protons in TMS yield an intense...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

A Lipid-Conjugation Strategy for Intracellular Reactive Oxygen Species Control in Hepatic Cells.

Angewandte Chemie (International ed. in English)·2026

Same authorSame journal

Moving NMR infrastructures to remote access capabilities.

Progress in nuclear magnetic resonance spectroscopy·2026

Same author

Accordion-like tuning of composite pulse dipolar recoupling in solid-state NMR.

The Journal of chemical physics·2026

Same author

Mobility of lactose in Milk powders.

Food research international (Ottawa, Ont.)·2026

Same author

Longitudinal Pulsed Dynamic Nuclear Polarization Transfer via Periodic Optimal Control.

The journal of physical chemistry letters·2026

Same author

Selective Mineral Recovery from Seawater by Ion-Exchangeable Metal-Organic Framework Glasses.

Journal of the American Chemical Society·2026

Same journal

Enhancing spin coherence times in solid-state NMR using tailored heteronuclear spin decoupling.

Progress in nuclear magnetic resonance spectroscopy·2026

Same journal

Band-selective excitation short transient <sup>1</sup>H PGSE NMR.

Progress in nuclear magnetic resonance spectroscopy·2026

Same journal

DNP-enhanced NMR of half-integer quadrupolar nuclei in solids.

Progress in nuclear magnetic resonance spectroscopy·2026

Same journal

NMR-based metabolomics: Where are we now and where are we going?

Progress in nuclear magnetic resonance spectroscopy·2025

Same journal

Experience of how to build an MRI machine from scratch.

Progress in nuclear magnetic resonance spectroscopy·2025

See all related articles

Search research articles

Related Experiment Video

Updated: Apr 5, 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

Solid-state NMR methods for oriented membrane proteins.

Sara K Hansen¹, Kresten Bertelsen¹, Berit Paaske¹

¹Center for Insoluble Protein Structures (inSPIN), Interdisciplinary Nanoscience Center (iNANO), Department of Chemistry, Aarhus University, Gustav Wieds Vej 14, DK-8000 Aarhus C, Denmark.

Progress in Nuclear Magnetic Resonance Spectroscopy

|August 19, 2015

Summary

This summary is machine-generated.

Oriented-sample solid-state NMR (ssNMR) is a powerful technique for studying membrane protein structures. This review covers 25 years of advancements in ssNMR methods and applications for membrane protein research.

Keywords:

Antimicrobial peptides Macroscopic orientation Membrane proteins Orientational restraints Oriented-sample solid-state NMR

More Related Videos

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

Contrast-Matching Detergent in Small-Angle Neutron Scattering Experiments for Membrane Protein Structural Analysis and Ab Initio Modeling

Contrast-Matching Detergent in Small-Angle Neutron Scattering Experiments for Membrane Protein Structural Analysis and Ab Initio Modeling

Published on: October 21, 2018

Related Experiment Videos

Last Updated: Apr 5, 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

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

Contrast-Matching Detergent in Small-Angle Neutron Scattering Experiments for Membrane Protein Structural Analysis and Ab Initio Modeling

Contrast-Matching Detergent in Small-Angle Neutron Scattering Experiments for Membrane Protein Structural Analysis and Ab Initio Modeling

Published on: October 21, 2018

Area of Science:

Biophysical Chemistry
Structural Biology
Membrane Biophysics

Background:

Oriented-sample solid-state NMR (ssNMR) is a key technique for characterizing membrane protein structures.
It provides insights into protein conformation within the cell membrane environment.
The method has been established for 25 years.

Purpose of the Study:

To review major developments in oriented-sample ssNMR over the past 25 years.
To highlight advancements in sample preparation, pulse sequences, and theoretical interpretation.
To showcase representative applications and future perspectives.

Main Methods:

Sample preparation techniques for oriented membranes.
Advanced solid-state NMR pulse sequences.
Theoretical frameworks for spectral interpretation.
Analysis of protein-lipid interactions and dynamics.

Main Results:

Significant progress in studying helix bundle membrane proteins and antimicrobial peptides.
Detailed characterization of protein-lipid interactions.
Derivation of information on membrane protein dynamics and anchoring.

Conclusions:

Oriented-sample ssNMR has matured into a versatile tool for membrane protein structure and dynamics.
Continued development promises further insights into complex membrane systems.
The review provides guidelines and perspectives for future research.