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

Protein Folding01:22

Protein Folding

129.4K
Overview
129.4K
Protein Folding01:25

Protein Folding

12.0K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
12.0K
Protein and Protein Structure02:15

Protein and Protein Structure

90.6K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
90.6K
Protein Organization01:24

Protein Organization

9.9K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
9.9K
Protein Organization01:13

Protein Organization

160.1K
Overview
160.1K
Protein Denaturation01:28

Protein Denaturation

10.2K
The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
10.2K

You might also read

Related Articles

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

Sort by
Same author

<i>mcstas_gisans</i>: combining ray tracing with the distorted-wave Born approximation using <i>McStas</i> and <i>BornAgain</i> for virtual GISANS experiments.

Journal of applied crystallography·2026
Same author

Twin-compartment solid-liquid cells for neutron reflectometry.

Journal of applied crystallography·2026
Same author

Surfactant self-assembly and micelle elongation in reline: structural basis and driving forces.

Philosophical transactions. Series A, Mathematical, physical, and engineering sciences·2026
Same author

Emergent reactance induced by the deformation of a current-driven skyrmion lattice.

Nature communications·2026
Same author

3D self-assembly of cyclic peptides into multilayered nanosheets.

Chemical science·2026
Same author

Influence of block microstructure on the interaction of styrene-maleic acid copolymer aggregates and lipid nanodiscs.

Soft matter·2026

Related Experiment Video

Updated: Mar 6, 2026

Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders
11:14

Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders

Published on: April 14, 2015

17.8K

Protein conformation in pure and hydrated deep eutectic solvents.

A Sanchez-Fernandez1, K J Edler2, T Arnold3

  • 1Department of Chemistry, University of Bath, Claverton Down, Bath, BA2 7AY, UK. a.sanchez.fernandez@bath.ac.uk and European Spallation Source, 221 00, Lund, Sweden.

Physical Chemistry Chemical Physics : PCCP
|March 17, 2017
PubMed
Summary

Deep eutectic solvents (DES) may preserve protein structure. This study investigated protein conformation in choline chloride-based DES and water mixtures using lysozyme and bovine serum albumin.

More Related Videos

Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro
10:01

Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro

Published on: April 8, 2020

6.4K
High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
08:48

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

Published on: April 28, 2022

2.2K

Related Experiment Videos

Last Updated: Mar 6, 2026

Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders
11:14

Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders

Published on: April 14, 2015

17.8K
Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro
10:01

Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro

Published on: April 8, 2020

6.4K
High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
08:48

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

Published on: April 28, 2022

2.2K

Area of Science:

  • Biophysics
  • Protein Science
  • Materials Science

Background:

  • Deep eutectic solvents (DES) are emerging as potential alternatives to water for biological applications.
  • Understanding protein behavior in non-aqueous environments is crucial for developing novel biotechnologies.

Purpose of the Study:

  • To investigate the conformational stability of proteins in choline chloride-based DES and their mixtures with water.
  • To explore the potential of DES as a medium for protein structure preservation.

Main Methods:

  • Circular dichroism (CD) spectroscopy was used to assess protein secondary and tertiary structures.
  • Small-angle neutron scattering (SANS) was employed to determine protein size and shape in solution.

Main Results:

  • Analysis of lysozyme and bovine serum albumin conformation in DES and water mixtures.
  • Data from CD and SANS provided insights into how DES affects protein structure.

Conclusions:

  • Choline chloride-based DES show potential for maintaining protein structure.
  • Further research is needed to fully elucidate protein-DES interactions and their implications.