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

71.1K
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...
71.1K
RNA Stability01:53

RNA Stability

35.7K
Intact DNA strands can be found in fossils, while scientists sometimes struggle to keep RNA intact under laboratory conditions. The structural variations between RNA and DNA underlie the differences in their stability and longevity. Because DNA is double-stranded, it is inherently more stable. The single-stranded structure of RNA is less stable but also more flexible and can form weak internal bonds. Additionally, most RNAs in the cell are relatively short, while DNA can be up to 250 million...
35.7K
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
Nuclear Stability03:18

Nuclear Stability

23.3K
Protons and neutrons, collectively called nucleons, are packed together tightly in a nucleus. With a radius of about 10−15 meters, a nucleus is quite small compared to the radius of the entire atom, which is about 10−10 meters. Nuclei are extremely dense compared to bulk matter, averaging 1.8 × 1014 grams per cubic centimeter. If the earth’s density were equal to the average nuclear density, the earth’s radius would be only about 200 meters.
To hold positively charged protons together...
23.3K
Problem-Solving: Tuning of a Guitar String01:04

Problem-Solving: Tuning of a Guitar String

1.1K
In the case of stringed instruments like the guitar, the elastic property that determines the speed of the sound produced is its linear mass density or the mass per unit length. This is simply called the linear density. If the string's linear density is constant along the string, then the linear density is simply the total mass divided by the total length.
The string's wave speed can be regulated by varying the linear density. Tension is the other property that determines the speed of...
1.1K
Stability01:28

Stability

418
The time response of a linear time-invariant (LTI) system can be divided into transient and steady-state responses. The transient response represents the system's initial reaction to a change in input and diminishes to zero over time. In contrast, the steady-state response is the behavior that persists after the transient effects have faded.
The stability of an LTI system is determined by the roots of its characteristic equation, known as poles. A system is stable if it produces a bounded...
418

You might also read

Related Articles

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

Sort by
Same author

Quantifying Ligand-to-Protein Distances in Complex Environments Using Intermolecular <sup>19</sup>F PRE NMR Spectroscopy.

Chembiochem : a European journal of chemical biology·2026
Same author

Non-hydrolyzable acetyllysine analogs to study protein acetylation in vitro and in cells.

Nature communications·2026
Same author

Fluorine Labeling and <sup>19</sup>F NMR Spectroscopy to Study Biological Molecules and Molecular Complexes.

Chemistry (Weinheim an der Bergstrasse, Germany)·2024
Same author

Thermostable WW-Domain Scaffold to Design Functional β-Sheet Miniproteins.

Journal of the American Chemical Society·2024
Same author

Including the Ensemble of Unstructured Conformations in the Analysis of Protein's Native State by High-Pressure NMR Spectroscopy.

Angewandte Chemie (International ed. in English)·2024
Same author

Targeted Preparation and NMR Spectroscopic Characterization of Lys11-Linked Ubiquitin Trimers.

Chembiochem : a European journal of chemical biology·2023

Related Experiment Video

Updated: Feb 1, 2026

In Vitro Model of Human Cutaneous Hypertrophic Scarring using Macromolecular Crowding
08:20

In Vitro Model of Human Cutaneous Hypertrophic Scarring using Macromolecular Crowding

Published on: May 1, 2020

7.2K

Macromolecular Crowding Tunes Protein Stability by Manipulating Solvent Accessibility.

Birgit Köhn1,2, Michael Kovermann1,2

  • 1Fachbereich Chemie, Universität Konstanz, Universitätsstrasse 10, 78457, Konstanz, Germany.

Chembiochem : a European Journal of Chemical Biology
|December 4, 2018
PubMed
Summary

Macromolecular crowding (MC) stabilizes proteins like Bacillus subtilis Cold shock protein B (BsCspB) against denaturation. This stabilization is concentration-dependent and linked to reduced solvent accessibility in protein loop regions.

Keywords:
NMR spectroscopybiophysicsmolecular crowdingprotein foldingthermodynamics

More Related Videos

Improving 2D and 3D Skin In Vitro Models Using Macromolecular Crowding
09:14

Improving 2D and 3D Skin In Vitro Models Using Macromolecular Crowding

Published on: August 22, 2016

13.0K
Staining of Proteins in Gels with Coomassie G-250 without Organic Solvent and Acetic Acid
07:47

Staining of Proteins in Gels with Coomassie G-250 without Organic Solvent and Acetic Acid

Published on: August 14, 2009

54.8K

Related Experiment Videos

Last Updated: Feb 1, 2026

In Vitro Model of Human Cutaneous Hypertrophic Scarring using Macromolecular Crowding
08:20

In Vitro Model of Human Cutaneous Hypertrophic Scarring using Macromolecular Crowding

Published on: May 1, 2020

7.2K
Improving 2D and 3D Skin In Vitro Models Using Macromolecular Crowding
09:14

Improving 2D and 3D Skin In Vitro Models Using Macromolecular Crowding

Published on: August 22, 2016

13.0K
Staining of Proteins in Gels with Coomassie G-250 without Organic Solvent and Acetic Acid
07:47

Staining of Proteins in Gels with Coomassie G-250 without Organic Solvent and Acetic Acid

Published on: August 14, 2009

54.8K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Protein structure and dynamics are crucial for intracellular processes.
  • Macromolecular crowding (MC) significantly influences these processes.
  • Understanding MC effects is key to comprehending cellular environments.

Purpose of the Study:

  • To investigate the impact of various macromolecular crowding (MC) agents on the stability of Bacillus subtilis Cold shock protein B (BsCspB).
  • To analyze the effects of MC during thermal and chemical denaturation.
  • To elucidate the mechanisms underlying MC-induced protein stabilization.

Main Methods:

  • Comprehensive analysis of protein denaturation under varying MC conditions.
  • Utilized Nuclear Magnetic Resonance (NMR) spectroscopy.
  • Monitored chemical shift (CS) perturbations and intramolecular hydrogen-bonding networks.
  • Assessed local protection of amide protons against solvent exchange.

Main Results:

  • Observed consistent stabilization of BsCspB across different MC agents.
  • Stabilization was dependent on MC concentration, not viscosity, polarity, or agent size.
  • NMR data revealed a pronounced reduction in amide proton exchange in loop regions.
  • CSs and hydrogen-bonding networks showed no systematic changes due to MC.

Conclusions:

  • Macromolecular crowding (MC) enhances protein stability in a concentration-dependent manner.
  • Reduced solvent accessibility in protein loop regions is a primary driver of MC-induced stabilization.
  • MC's influence on protein stability is a general phenomenon, independent of specific crowding agent properties.