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

Search research articles

Related Experiment Videos

UV-visible derivative spectroscopy under high pressure.

Reinhard Lange¹, Claude Balny

¹INSERM, Unité 128, IFR 24, CNRS, Montpellier, France.

Biochimica Et Biophysica Acta

|May 2, 2002

Summary

High hydrostatic pressure alters protein structure and interactions. Ultraviolet derivative spectroscopy, adapted for high pressure, can detect these protein changes, revealing both its capabilities and limitations.

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

Evidence for Specific Receptor-Mediated Toxicity of Pharmaceuticals in Aquatic Organisms Derived from Acute and Chronic Standard Endpoints.

Environmental toxicology and chemistry·2021

Same author

Effects of the Gestagen Levonorgestrel in a Life Cycle Test with Zebrafish (Danio rerio).

Environmental toxicology and chemistry·2021

Same author

Equilibria of oligomeric proteins under high pressure - A theoretical description.

Journal of theoretical biology·2016

Same author

Getting to the core of prion superstructural variability.

Prion·2015

Same author

The Volumetric Diversity of Misfolded Prion Protein Oligomers Revealed by Pressure Dissociation.

The Journal of biological chemistry·2015

Same author

Inhibitor and substrate binding induced stability of HIV-1 protease against sequential dissociation and unfolding revealed by high pressure spectroscopy and kinetics.

PloS one·2015

Area of Science:

Biophysics
Protein Chemistry
Spectroscopy

Background:

High hydrostatic pressure (HHP) significantly impacts protein structure, including interactions, conformation, and solvation.
Understanding these pressure-induced alterations is crucial for various biological and industrial applications.

Purpose of the Study:

To explore the utility of ultraviolet derivative spectroscopy for detecting pressure-induced changes in proteins.
To demonstrate the potential and limitations of this technique in high-pressure environments.

Main Methods:

Adaptation of ultraviolet derivative spectroscopy for high-pressure experimental setups.
Application of the adapted spectroscopy to analyze selected protein samples under varying hydrostatic pressures.

Main Results:

Ultraviolet derivative spectroscopy effectively detects alterations in protein intra- and intermolecular interactions, conformation, and solvation under high hydrostatic pressure.
The study highlights specific examples showcasing the technique's capabilities and identifies its inherent limitations.

Conclusions:

Adapted ultraviolet derivative spectroscopy is a valuable tool for investigating pressure effects on proteins.
Further development may enhance its application scope in high-pressure protein research.

Related Experiment Videos