Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)01:20

¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)

1.3K
When proton-coupled carbon-13 spectra are simplified by a broadband proton decoupling technique, structural information about the coupled protons is lost. Distortionless enhancement by polarization transfer (DEPT) is a technique that provides information on the number of hydrogens attached to each carbon in a molecule. While the DEPT experiment utilizes complex pulse sequences, the pulse delay and flip angle are specifically manipulated. The resulting signals have different phases depending on...
1.3K
Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

4.7K
Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
4.7K
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

4.3K
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
4.3K
Aquaporins01:25

Aquaporins

5.0K
Aquaporins or AQPs are a family of integral membrane proteins whose primary function is to transport water, while some called aquaglyceroporins also transport glycerol. In addition, aquaporins have also been suspected to be involved in transporting volatile substances, such as carbon dioxide and ammonia, across membranes. Such AQPs that act as gas channels are often highly expressed in cells involved in the gaseous exchange, such as red blood cells, epithelial cells, and pulmonary capillaries.
5.0K
Membrane Fluidity01:23

Membrane Fluidity

149.8K
Cell membranes are composed of phospholipids, proteins, and carbohydrates loosely attached to one another through chemical interactions. Molecules are generally able to move about in the plane of the membrane, giving the membrane its flexible nature called fluidity. Two other features of the membrane contribute to membrane fluidity: the chemical structure of the phospholipids and the presence of cholesterol in the membrane.
149.8K
Membrane Fluidity01:26

Membrane Fluidity

13.8K
Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
Mosaic nature of the membrane
The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is...
13.8K

You might also read

Related Articles

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

Sort by
Same author

Is synuclein aggregation a derived or ancestral trait? Ancestral sequence reconstruction uncovers stepwise evolution of synuclein aggregation.

bioRxiv : the preprint server for biology·2025
Same author

Real-time single-molecule observation of incipient collagen fibrillogenesis and remodeling.

Proceedings of the National Academy of Sciences of the United States of America·2024
Same author

Structure of the nonhelical filament of the Alzheimer's disease tau core.

Proceedings of the National Academy of Sciences of the United States of America·2023
Same author

Oxycodone withdrawal is associated with increased cocaine self-administration and aberrant accumbens glutamate plasticity in rats.

Neuropharmacology·2023
Same author

Atomic structure of the open SARS-CoV-2 E viroporin.

Science advances·2023
Same author

Is Short-Course Antibiotic Therapy Suitable for Pseudomonas aeruginosa Bloodstream Infections in Onco-hematology Patients With Febrile Neutropenia? Results of a Multi-institutional Analysis.

Clinical infectious diseases : an official publication of the Infectious Diseases Society of America·2023

Related Experiment Video

Updated: Apr 23, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

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

Published on: September 17, 2017

16.8K

Probing membrane protein structure using water polarization transfer solid-state NMR.

Jonathan K Williams1, Mei Hong1

  • 1Department of Chemistry, Iowa State University, Ames, IA 50011, United States.

Journal of Magnetic Resonance (San Diego, Calif. : 1997)
|September 18, 2014
PubMed
Summary
This summary is machine-generated.

Solid-state NMR detects water polarization transfer to biomolecules, revealing hydration and structure. This technique offers insights into protein, membrane, and carbohydrate interactions for biological systems.

Keywords:
Chemical exchangeHeteronuclear correlationInfluenza M2 proteinIon channelsSpin diffusion

More Related Videos

Probing the Structure and Dynamics of Interfacial Water with Scanning Tunneling Microscopy and Spectroscopy
10:28

Probing the Structure and Dynamics of Interfacial Water with Scanning Tunneling Microscopy and Spectroscopy

Published on: May 27, 2018

8.4K
Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

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

Published on: March 5, 2017

12.8K

Related Experiment Videos

Last Updated: Apr 23, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

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

Published on: September 17, 2017

16.8K
Probing the Structure and Dynamics of Interfacial Water with Scanning Tunneling Microscopy and Spectroscopy
10:28

Probing the Structure and Dynamics of Interfacial Water with Scanning Tunneling Microscopy and Spectroscopy

Published on: May 27, 2018

8.4K
Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

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

Published on: March 5, 2017

12.8K

Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • Water is crucial for biological macromolecule structure and function.
  • Solid-state NMR (Nuclear Magnetic Resonance) enables studying water-biomolecule interactions.
  • Heteronuclear-detected (1)H polarization transfer is a key technique.

Purpose of the Study:

  • To review radiofrequency pulse sequences for water polarization transfer.
  • To elucidate mechanisms of polarization transfer (chemical exchange, spin diffusion, NOE).
  • To showcase applications in diverse biological systems.

Main Methods:

  • Review of radiofrequency pulse sequences for water polarization transfer.
  • Analysis of polarization transfer mechanisms under varying conditions (temperature, magic-angle-spinning, pulse irradiation).
  • Application of the technique to study hydration and structure of biomolecules.

Main Results:

  • Chemical exchange is a universal mechanism; spin diffusion is key within macromolecules.
  • Tightly bound water is rare in proteins at ambient temperatures.
  • Water polarization transfer reveals hydration of proteins, membranes, and polysaccharides.
  • Atomic-resolution details of ion conduction kinetics and mechanisms were obtained.
  • Structure of influenza M2 protein proton channel determined via water polarization transfer.
  • Transfer rates provide secondary structure, helix tilt, and oligomeric information.

Conclusions:

  • Water polarization transfer is a versatile method for studying water-biomolecule interactions.
  • The technique provides site-specific, structure-related information, especially for membrane proteins.
  • It offers insights into biological processes like ion conduction and protein structure.