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

Problem Solving on Stress and Strain01:22

Problem Solving on Stress and Strain

Stress is a quantity that describes the magnitude of a force that causes deformation, generally defined as internal force per unit area. When forces pull on an object and cause its elongation, like the stretching of an elastic band, it is called tensile stress. When forces cause the compression of an object, it is known as compressive stress. When an object is being squeezed uniformly from all sides, like a submarine in the depths of the ocean, we call this kind of stress bulk stress (or volume...
SDS-PAGE01:27

SDS-PAGE

Gel electrophoresis is a method that separates biological macromolecules like nucleic acids or proteins by forcing them to pass through a gel matrix under an electric field.
A variation of gel electrophoresis, termed  polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact proteins...
Protein Denaturation01:28

Protein Denaturation

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...
Shearing Stress01:18

Shearing Stress

Shearing stress, denoted by the Greek letter tau (τ), is stress caused by forces acting transversely on an object. These forces create internal ones within the entity in the plane where the external forces are applied. The resultant of these internal forces is the shear in the section.
The average shearing stress can be calculated by dividing the shear by the area of the cross-section.
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein Folding

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...

You might also read

Related Articles

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

Sort by
Same author

Advocating for a "Community to bench model" in the 21st century.

EBioMedicine·2020
Same author

High-flow nasal therapy - modelling the mechanism.

Anaesthesia·2019
Same author

Neoadjuvant chemoradiotherapy with concurrent cisplatin/5-fluorouracil is associated with increased pathologic complete response and improved survival compared to carboplatin/paclitaxel in patients with locally advanced esophageal cancer.

Diseases of the esophagus : official journal of the International Society for Diseases of the Esophagus·2017
Same author

Preoperative carboplatin and paclitaxel-based chemoradiotherapy for esophageal carcinoma: results of a modified CROSS regimen utilizing radiation doses greater than 41.4 Gy.

Diseases of the esophagus : official journal of the International Society for Diseases of the Esophagus·2015
Same author

New methodology, tools, and protocolized analysis are needed to advance individualized treatment paradigms in esophageal cancer.

Diseases of the esophagus : official journal of the International Society for Diseases of the Esophagus·2014
Same author

Margin width is not predictive of residual disease on re-excision in breast conserving therapy.

Journal of surgical oncology·2013

Related Experiment Video

Updated: Jun 6, 2026

Ensemble Force Spectroscopy by Shear Forces
07:30

Ensemble Force Spectroscopy by Shear Forces

Published on: July 26, 2022

Effects of shear on proteins in solution.

C R Thomas1, D Geer

  • 1School of Chemical Engineering, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK. c.r.thomas@bham.ac.uk

Biotechnology Letters
|November 19, 2010
PubMed
Summary

Shear forces alone rarely damage proteins in solution. Instead, damage often results from interfacial phenomena, such as moving gas-liquid interfaces or nanoparticles, impacting therapeutic protein quality and patient safety.

Area of Science:

  • Biochemistry
  • Protein Chemistry
  • Fluid Mechanics

Background:

  • Decades of research have investigated protein denaturation by shear during processing.
  • Recent concerns focus on the impact of shear and related effects on therapeutic protein quality.

Purpose of the Study:

  • To clarify the mechanisms of protein damage in solution during processing.
  • To differentiate between true shear effects and interfacial phenomena.

Main Methods:

  • Review of historical and recent research on protein behavior under mechanical stress.
  • Analysis of fluid mechanical shear versus interfacial phenomena.

Main Results:

  • Fluid mechanical shear alone is unlikely to damage most proteins.

More Related Videos

Characterizing Single-Molecule Conformational Changes Under Shear Flow with Fluorescence Microscopy
08:47

Characterizing Single-Molecule Conformational Changes Under Shear Flow with Fluorescence Microscopy

Published on: January 25, 2020

A Uniform Shear Assay for Human Platelet and Cell Surface Receptors via Cone-plate Viscometry
04:32

A Uniform Shear Assay for Human Platelet and Cell Surface Receptors via Cone-plate Viscometry

Published on: June 5, 2019

Related Experiment Videos

Last Updated: Jun 6, 2026

Ensemble Force Spectroscopy by Shear Forces
07:30

Ensemble Force Spectroscopy by Shear Forces

Published on: July 26, 2022

Characterizing Single-Molecule Conformational Changes Under Shear Flow with Fluorescence Microscopy
08:47

Characterizing Single-Molecule Conformational Changes Under Shear Flow with Fluorescence Microscopy

Published on: January 25, 2020

A Uniform Shear Assay for Human Platelet and Cell Surface Receptors via Cone-plate Viscometry
04:32

A Uniform Shear Assay for Human Platelet and Cell Surface Receptors via Cone-plate Viscometry

Published on: June 5, 2019

  • Moving gas-liquid interfaces are particularly detrimental to protein stability.
  • Protein aggregation on nanoparticles from solid surfaces is a significant safety concern.
  • Conclusions:

    • Labeling all protein damage as "shear" is inaccurate and hinders understanding.
    • Interfacial phenomena, not shear itself, are the primary drivers of protein damage in many processing scenarios.
    • Accurate identification of damage mechanisms is crucial for ensuring therapeutic protein quality and patient safety.