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

Crossover Experiments

Crossover Experiments

Crossover experiments, also called the repeated-measurements design, is a study design in which all experimental units are exposed to all treatments in different periods. Crossover experiments are generally used in psychology, the pharmaceutical industry, agriculture, and medicine.
Crossover designs are performed even with smaller sample sizes since the samples can act as their controls. These are better than simple randomized trials since patients are exposed to all the treatments.

Cross-reactivity

Cross-reactivity

Double Resonance Techniques: Overview

Double Resonance Techniques: Overview

Double resonance techniques in Nuclear Magnetic Resonance (NMR) spectroscopy involve the simultaneous application of two different frequencies or radiofrequency pulses to manipulate and observe two distinct nuclear spins. One important application of double resonance is spin decoupling, which selectively suppresses coupling with one type of nucleus while observing the NMR signal from another nucleus, simplifying the spectrum and enhancing resolution.
Spin decoupling is usually achieved by...

You might also read

Related Articles

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

Sort by

Same author

Allosteric Targeting of the ACE2 Dimer Interface by a Medium-sized Compound Inhibits SARS-CoV-2 Entry.

Journal of molecular biology·2026

Same author

Phase Separation Driven by Dynamic Interactions in the N-Terminal Intrinsically Disordered Region of the DEAD-Box RNA Helicase DDX3X.

Journal of the American Chemical Society·2026

Same author

Direct binding of the neurorehabilitation drug edonerpic maleate to CRMP2 demonstrated by NMR spectroscopy.

Neuroscience research·2026

Same author

Aggregation-State Dynamics Drive Double Cooperativity Between Antimicrobial Peptides LL-37 and HNP1.

Angewandte Chemie (International ed. in English)·2026

Same author

Polypharmacologic phosphoinositide modulation by FTY720 triggers endomembrane trafficking collapse and metabolic starvation in cancer cells.

Biochemical and biophysical research communications·2026

Same author

NMR investigation of the sliding motion of RNA helicase DDX3X along single-stranded RNA.

Biophysical chemistry·2026

Same journal

Lasing emission spectroscopy for bioanalytics and biomedicine.

Quarterly reviews of biophysics·2026

Same journal

Elementary processes and mechanisms of nanopore formation induced by antimicrobial peptides and other membrane-active peptides.

Quarterly reviews of biophysics·2026

Same journal

Biomineralization: Perspectives on control of crystal polymorphism, order-disorder and solvation states.

Quarterly reviews of biophysics·2026

Same journal

The pivotal roles of cellular biophysics and mechanobiology in the development of Human Organs-on-Chips.

Quarterly reviews of biophysics·2026

Same journal

Biophysics meets fungal biology: Characterising the fungal cell envelope and its interactions with drug-like molecules.

Quarterly reviews of biophysics·2026

Same journal

Energy landscapes in molecular biology: History, principles, and perspectives.

Quarterly reviews of biophysics·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Apr 30, 2026

Spin Saturation Transfer Difference NMR SSTD NMR: A New Tool to Obtain Kinetic Parameters of Chemical Exchange Processes

Spin Saturation Transfer Difference NMR SSTD NMR: A New Tool to Obtain Kinetic Parameters of Chemical Exchange Processes

Published on: November 12, 2016

Cross-saturation and transferred cross-saturation experiments.

Takumi Ueda¹, Koh Takeuchi², Noritaka Nishida¹

¹Graduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo, Tokyo 113-0033, Japan.

Quarterly Reviews of Biophysics

|May 1, 2014

Summary

This summary is machine-generated.

New nuclear magnetic resonance techniques, cross-saturation (CS) and transferred cross-saturation (TCS), precisely identify protein-protein interaction interfaces. These methods enable structural analysis of large, heterogeneous complexes under physiological conditions for drug development and biological understanding.

More Related Videos

Glutamine Flux Imaging Using Genetically Encoded Sensors

Glutamine Flux Imaging Using Genetically Encoded Sensors

Published on: July 31, 2014

Dual-Color Fluorescence Cross-Correlation Spectroscopy to Study Protein-Protein Interaction and Protein Dynamics in Live Cells

Dual-Color Fluorescence Cross-Correlation Spectroscopy to Study Protein-Protein Interaction and Protein Dynamics in Live Cells

Published on: December 11, 2021

Related Experiment Videos

Last Updated: Apr 30, 2026

Spin Saturation Transfer Difference NMR SSTD NMR: A New Tool to Obtain Kinetic Parameters of Chemical Exchange Processes

Spin Saturation Transfer Difference NMR SSTD NMR: A New Tool to Obtain Kinetic Parameters of Chemical Exchange Processes

Published on: November 12, 2016

Glutamine Flux Imaging Using Genetically Encoded Sensors

Glutamine Flux Imaging Using Genetically Encoded Sensors

Published on: July 31, 2014

Dual-Color Fluorescence Cross-Correlation Spectroscopy to Study Protein-Protein Interaction and Protein Dynamics in Live Cells

Dual-Color Fluorescence Cross-Correlation Spectroscopy to Study Protein-Protein Interaction and Protein Dynamics in Live Cells

Published on: December 11, 2021

Area of Science:

Biochemistry
Structural Biology
Biophysics

Background:

Structural analysis of protein-protein interactions is vital for understanding biological mechanisms and drug development.
Conventional methods struggle with large, heterogeneous, or membrane-bound protein complexes under physiological conditions.

Purpose of the Study:

To introduce and discuss the cross-saturation (CS) and transferred cross-saturation (TCS) nuclear magnetic resonance (NMR) techniques.
To highlight the utility of CS and TCS for analyzing protein-protein complex interfaces.
To review recent advancements and applications of these NMR methods.

Main Methods:

Development of the cross-saturation (CS) NMR technique for identifying protein-protein interaction interfaces.
Extension of CS to transferred cross-saturation (TCS) for analyzing large (>150 kDa) and heterogeneous complexes under fast exchange conditions (>0.1 s(-1)).

Main Results:

CS and TCS enable precise identification of protein-protein complex interfaces.
TCS is effective for studying large, heterogeneous protein complexes in physiologically relevant states.
These methods facilitate the construction of accurate protein-protein complex models.

Conclusions:

CS and TCS are powerful NMR tools for structural analysis of challenging protein complexes.
These techniques advance the understanding of protein interactions in native-like environments.
Applications include in situ analysis of biologically and medically significant proteins.