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

You might also read

Related Articles

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

Sort by

Same author

The Cytosolic Zinc Finger Domain Structure of the CCHFV Glycoprotein n Is Maintained in Its Membrane-Bound Form.

Journal of the American Chemical Society·2026

Same author

An engineered closed-shell, two-component, 480-subunit nucleocapsid.

Proceedings of the National Academy of Sciences of the United States of America·2026

Same author

Structural transport and inhibition mechanism of the mitochondrial pyruvate carrier.

Trends in biochemical sciences·2025

Same author

The peculiar properties of mitochondrial carriers of the SLC25 family.

The Biochemical journal·2025

Same author

NMR side-chain assignments of the Crimean-Congo hemorrhagic fever virus glycoprotein n cytosolic domain.

Magnetic resonance (Gottingen, Germany)·2025

Same author

NMR Structural Characterization of SARS-CoV-2 ORF6 Reveals an N-Terminal Membrane Anchor.

Journal of the American Chemical Society·2025

Search research articles

Related Experiment Video

Updated: Dec 26, 2025

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

Published on: April 2, 2015

Sedimentation Yields Long-Term Stable Protein Samples as Shown by Solid-State NMR.

Thomas Wiegand¹, Denis Lacabanne¹, Anahit Torosyan¹

¹Physical Chemistry, ETH Zürich, Zurich, Switzerland.

Frontiers in Molecular Biosciences

|March 11, 2020

Summary

This summary is machine-generated.

Sedimenting proteins into magic-angle spinning (MAS) rotors enables fast sample preparation for solid-state Nuclear Magnetic Resonance (NMR). This method ensures protein stability and function for years, crucial for studying complex biological molecules.

Keywords:

nucleotides proteins sedimentation solid-state NMR stability

More Related Videos

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

Measuring Protein Binding to F-actin by Co-sedimentation

Measuring Protein Binding to F-actin by Co-sedimentation

Published on: May 18, 2017

Related Experiment Videos

Last Updated: Dec 26, 2025

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

Published on: April 2, 2015

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

Measuring Protein Binding to F-actin by Co-sedimentation

Measuring Protein Binding to F-actin by Co-sedimentation

Published on: May 18, 2017

Area of Science:

Biophysics
Structural Biology
Biochemistry

Background:

Solid-state Nuclear Magnetic Resonance (NMR) is vital for studying non-crystalline proteins.
Magic-angle spinning (MAS) rotors allow fast and reliable sample preparation.
High protein concentrations (up to 400 mg/mL) are achievable in MAS rotors.

Purpose of the Study:

To assess the long-term stability of sedimented proteins in MAS rotors.
To evaluate the structural and functional integrity of proteins after prolonged storage.
To demonstrate the utility of sedimented proteins for multi-year solid-state NMR studies.

Main Methods:

Protein sedimentation into MAS rotors.
Solid-state NMR spectroscopy.
Functional assays for protein activity.

Main Results:

Four different proteins and their complexes (bacterial DnaB helicase, ABC transporter, archaeal primase, RNA polymerase subunit) were sedimented.
No spectral differences or signal intensity loss were observed in solid-state NMR spectra over 5 years.
An ABC transporter maintained both structure and function after long-term storage in the sedimented state.

Conclusions:

Sedimented proteins in MAS rotors exhibit long-term stability over several years.
This technique preserves both the structure and function of proteins, enabling extended NMR investigations.
Protein sedimentation is a robust method for preparing stable samples for solid-state NMR analysis.