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

Solvents01:12

Solvents

71.4K
A solvent is a substance, most often a liquid, that can dissolve other substances. Here, the substance being dissolved is called a solute. When a solvent and a solute combine, they form a solution - a homogenous mixture of both the solvent and the solute. Water is a universal biological solvent. Its polar structure allows it to dissolve many other polar compounds. The ability of water to dissolve is governed by a balance between water molecules binding to each other and binding to the solute.
A...
71.4K
Titration in Nonaqueous Solvents01:16

Titration in Nonaqueous Solvents

1.4K
Most acid-base titrations are performed in an aqueous medium. In aqueous titrations, water competes with weaker acids or bases for proton donation or acceptance, leading to ambiguous endpoints in the titration curve. Water also affects the partial ionization of weak acids or bases. For example, water accepts a proton from acetic acid to form hydronium and acetate ions. The hydronium ion formed is a stronger acid than acetic acid, and the acetate ion is a stronger base than water. As a result,...
1.4K
Factors Affecting Protein-Drug Binding: Drug Interactions01:23

Factors Affecting Protein-Drug Binding: Drug Interactions

617
Drug interactions are a critical aspect of pharmacology and can occur when two or more drugs compete for the same binding site. This competition can result in one drug displacing another, altering the effect of the displaced drug. Drug interactions are complex processes that rely heavily on how much of the displacer drug is present and how strongly it can bind to the same sites as the displaced drug.
Displacement interactions can have varying outcomes, ranging from toxicity to virtually...
617
Protein-protein Interfaces02:04

Protein-protein Interfaces

14.8K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.8K
Protein and Protein Structure02:15

Protein and Protein Structure

88.9K
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...
88.9K
Chemical Shift: Internal References and Solvent Effects01:17

Chemical Shift: Internal References and Solvent Effects

1.4K
In an NMR sample, precise measurement of the absolute absorption frequencies of nuclei is difficult. A standard internal reference compound is added, and the frequency difference between the reference signal and sample signals is measured.
The internal reference compound generally used in NMR spectroscopy is tetramethylsilane (TMS). TMS is preferred because it is chemically inert, soluble in NMR solvents, and easily removable. Also, the highly shielded methyl protons in TMS yield an intense...
1.4K

You might also read

Related Articles

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

Sort by
Same author

Editorial for Special Issue "Recombinant Proteins for Molecular Biology Research: Technologies and Applications".

Current issues in molecular biology·2026
Same author

Parameter optimization for circular dichroism spectroscopy of proteins: A practical approach for rapid acquisition of high-quality spectra.

Analytical biochemistry·2026
Same author

A robust and sensitive method for detecting subtle structural differences in bovine serum albumin.

BioTechniques·2026
Same author

Effects of Arginine on Hierarchical Protein Aggregation.

The protein journal·2026
Same author

Differences and Similarities in Protein and Nucleic Acid Structures and Their Biological Interactions.

Current issues in molecular biology·2026
Same author

Non-ionic Detergent-Assisted Refolding of Protein from Protein-SDS Complex.

The protein journal·2025

Related Experiment Video

Updated: Feb 12, 2026

Synthesis of Esters Via a Greener Steglich Esterification in Acetonitrile
06:52

Synthesis of Esters Via a Greener Steglich Esterification in Acetonitrile

Published on: October 30, 2018

37.6K

Acetonitrile as solvent for protein interaction analysis.

Tsutomu Arakawa1

  • 1Alliance Protein Laboratories, a Division of KBI Biopharma, 6042 Cornerstone Court West, San Diego, 92121, CA.

International Journal of Biological Macromolecules
|April 2, 2018
PubMed
Summary
This summary is machine-generated.

Dimethyl sulfoxide (DMSO) can interfere with structural analysis. Acetonitrile (ACN) offers a viable alternative for dissolving hydrophobic compounds in spectroscopic studies, showing comparable dissolution but superior far UV circular dichroism performance.

Keywords:
AcetonitrileCircular dichroismDimethyl sulfoxideDissolutionDrug substance

More Related Videos

Organic Solvent-Based Protein Precipitation for Robust Proteome Purification Ahead of Mass Spectrometry
11:12

Organic Solvent-Based Protein Precipitation for Robust Proteome Purification Ahead of Mass Spectrometry

Published on: February 7, 2022

12.4K
A Protein Preparation Method for the High-throughput Identification of Proteins Interacting with a Nuclear Cofactor Using LC-MS/MS Analysis
05:43

A Protein Preparation Method for the High-throughput Identification of Proteins Interacting with a Nuclear Cofactor Using LC-MS/MS Analysis

Published on: January 24, 2017

9.0K

Related Experiment Videos

Last Updated: Feb 12, 2026

Synthesis of Esters Via a Greener Steglich Esterification in Acetonitrile
06:52

Synthesis of Esters Via a Greener Steglich Esterification in Acetonitrile

Published on: October 30, 2018

37.6K
Organic Solvent-Based Protein Precipitation for Robust Proteome Purification Ahead of Mass Spectrometry
11:12

Organic Solvent-Based Protein Precipitation for Robust Proteome Purification Ahead of Mass Spectrometry

Published on: February 7, 2022

12.4K
A Protein Preparation Method for the High-throughput Identification of Proteins Interacting with a Nuclear Cofactor Using LC-MS/MS Analysis
05:43

A Protein Preparation Method for the High-throughput Identification of Proteins Interacting with a Nuclear Cofactor Using LC-MS/MS Analysis

Published on: January 24, 2017

9.0K

Area of Science:

  • Biochemistry and Biophysics
  • Spectroscopic Analysis
  • Drug Discovery and Development

Background:

  • Dimethyl sulfoxide (DMSO) is a common solvent for hydrophobic and aromatic compounds in drug screening.
  • DMSO's strong absorbance in the far UV region can interfere with structural evaluation using techniques like circular dichroism (CD).
  • Acetonitrile (ACN) is widely used in chromatography for proteins and small organic molecules.

Purpose of the Study:

  • To evaluate acetonitrile (ACN) as an alternative solvent to dimethyl sulfoxide (DMSO) for sample preparation in spectroscopic analyses.
  • To compare the dissolution capabilities of DMSO and ACN for hydrophobic compounds.
  • To assess the performance of ACN versus DMSO in far UV circular dichroism (CD) measurements.

Main Methods:

  • A side-by-side comparison of DMSO and ACN as solvents.
  • Use of dodecyl-gallate (a small aromatic/hydrophobic molecule) and bovine serum albumin as a model system.
  • Evaluation of dissolution capability and far UV circular dichroism (CD) performance for both solvents.

Main Results:

  • Both DMSO and ACN demonstrated capability in dissolving the model hydrophobic compound, dodecyl-gallate.
  • ACN exhibited significantly better performance in far UV circular dichroism (CD) measurements compared to DMSO.
  • The strong absorbance of DMSO in the far UV region was confirmed as a limitation for CD spectroscopy.

Conclusions:

  • Acetonitrile (ACN) is a suitable alternative solvent to dimethyl sulfoxide (DMSO) for preparing samples for structural evaluation.
  • ACN offers superior performance for far UV circular dichroism (CD) studies, minimizing solvent-related spectral interference.
  • The findings support the use of ACN in drug discovery workflows involving both dissolution and spectroscopic structural analysis.