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

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...
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
Protein and Protein Structure02:15

Protein and Protein Structure

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 can...
RNA Stability01:53

RNA Stability

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...
RNA Stability01:53

RNA Stability

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...

You might also read

Related Articles

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

Sort by
Same author

Eco-friendly synthesis and evaluation of carbon dots from kitchen waste for potential antibacterial applications.

Scientific reports·2026
Same author

Corrigendum to 'Biosynthesis, characterisation and biocompatibility of a unique and elastomeric medium chain-length polyhydroxyalkanoate for kidney glomerular tissue engineering' [Mater. Today Bio 33 (2025), 101932].

Materials today. Bio·2026
Same author

Heat Shock Proteins as Cancer Biomarkers: From Mechanism to Clinical Application.

Molecular diagnosis & therapy·2026
Same author

Modulation of biomolecular condensation of alpha-synuclein variants by eprodisate.

Communications chemistry·2026
Same author

Therapeutic aptamers in drug discovery: future elements of the pharmaceutical arsenal?

Expert opinion on drug discovery·2026
Same author

Optimisation of electrospinning parameters to successfully obtain high ratios of medium chain length polyhydroxyalkanoate in electrospun fibres with drug loading for wound healing applications.

Journal of materials science. Materials in medicine·2026

Related Experiment Video

Updated: Jun 16, 2026

Rapid One-step Enzymatic Synthesis and All-aqueous Purification of Trehalose Analogues
09:27

Rapid One-step Enzymatic Synthesis and All-aqueous Purification of Trehalose Analogues

Published on: February 17, 2017

Trehalose and protein stability.

Nishant Kumar Jain1, Ipsita Roy

  • 1Department of Biotechnology, National Institute of Pharmaceutical Education and Research (NIPER), S.A.S. Nagar, Punjab, India.

Current Protocols in Protein Science
|February 16, 2010
PubMed
Summary
This summary is machine-generated.

Trehalose stabilizes proteins against stress by preventing aggregation. Its unique properties protect proteins, maintaining their active form under adverse conditions.

More Related Videos

Purification of the Sarco-Endoplasmic Reticulum Ca2+-ATPase from Rabbit Muscle
08:37

Purification of the Sarco-Endoplasmic Reticulum Ca2+-ATPase from Rabbit Muscle

Published on: March 21, 2025

Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen
08:13

Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen

Published on: March 4, 2017

Related Experiment Videos

Last Updated: Jun 16, 2026

Rapid One-step Enzymatic Synthesis and All-aqueous Purification of Trehalose Analogues
09:27

Rapid One-step Enzymatic Synthesis and All-aqueous Purification of Trehalose Analogues

Published on: February 17, 2017

Purification of the Sarco-Endoplasmic Reticulum Ca2+-ATPase from Rabbit Muscle
08:37

Purification of the Sarco-Endoplasmic Reticulum Ca2+-ATPase from Rabbit Muscle

Published on: March 21, 2025

Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen
08:13

Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen

Published on: March 4, 2017

Area of Science:

  • Biochemistry
  • Protein Science
  • Molecular Biology

Background:

  • Proteins are susceptible to unfolding and aggregation under various stress conditions, leading to loss of function.
  • Osmolytes, particularly trehalose, are known to play a crucial role in protein stabilization.
  • Understanding these stabilization mechanisms is vital for biotechnology and medicine.

Purpose of the Study:

  • To discuss the adverse conditions that cause protein aggregation and inactivation.
  • To examine the role of trehalose in stabilizing proteins and maintaining their functional activity.
  • To present theories explaining trehalose's protective action and discuss experimental tools.

Main Methods:

  • Literature review of trehalose's physical and chemical properties.
  • Analysis of mechanisms underlying protein aggregation under stress.
  • Discussion of experimental techniques for studying protein aggregation and trehalose's role.

Main Results:

  • Trehalose's properties (low reactivity, high glass transition temperature, water affinity) make it ideal for stabilizing proteins.
  • Trehalose effectively inhibits protein aggregation and maintains protein structure and function under stress.
  • Various theories explain trehalose's protective effects, including preferential hydration and exclusion from the protein surface.

Conclusions:

  • Trehalose is a highly effective osmolyte for protein stabilization against stress-induced aggregation.
  • Its unique physicochemical properties contribute to its protective capabilities.
  • Further research using experimental tools can elucidate the precise mechanisms of trehalose's action.