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 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...
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
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...
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...
Protein Folding01:22

Protein Folding

Overview

You might also read

Related Articles

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

Sort by
Same author

PON-Del predictor for sequence retaining protein deletions.

PLoS computational biology·2026
Same author

Late-Stage Diagnosis of Biliary Atresia in Rural America.

Cureus·2026
Same author

Pediatric Drug-Induced Sleep Endoscopy Directed Surgery Outcomes With Trisomy 21 Subgroup Comparison: A Meta-Analysis.

Otolaryngology--head and neck surgery : official journal of American Academy of Otolaryngology-Head and Neck Surgery·2026
Same author

The Oura Ring Versus Medical-Grade Sleep Studies: A Systematic Review and Meta-Analysis.

OTO open·2025
Same author

Proteome-Wide Analysis of Human Deletions.

Proteins·2025
Same author

ProToxin, a Predictor of Protein Toxicity.

Toxins·2025
Same journal

COL1A1 and SERPINE1 as Potential Therapeutic Targets in Diabetic Retinopathy: A Study Incorporating RNA Transcriptomics, Single-Cell RNA Sequencing, and Proteomics.

Human mutation·2026
Same journal

Autosomal Dominant Missense <i>DAG1</i> Variant Linked to Mild-Moderate LGMD R16.

Human mutation·2026
Same journal

RETRACTION: "Differential Effects of AKT1(p.E17K) Expression on Human Mammary Luminal Epithelial and Myoepithelial Cells".

Human mutation·2026
Same journal

Diagnostic Yield of Genome Sequencing in an Iranian Exome-Negative Autosomal-Recessive Intellectual Disability Cohort.

Human mutation·2026
Same journal

Exploring the Functional Impact of Individual <i>DDX41</i> Variants With a Fast and Robust Cell-Based Method.

Human mutation·2026
Same journal

Modeling the Effects of Single Nucleotide Polymorphisms (SNPs) on the Structure and Function of the Human <i>RET</i> Gene: An In Silico Study.

Human mutation·2026
See all related articles

Related Experiment Video

Updated: Jun 15, 2026

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project
07:22

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project

Published on: February 11, 2019

Performance of protein stability predictors.

Sofia Khan1, Mauno Vihinen

  • 1Institute of Medical Technology, FI-33014 University of Tampere, Finland.

Human Mutation
|March 17, 2010
PubMed
Summary
This summary is machine-generated.

This study evaluated 11 protein stability predictors for mutation effects. While some tools like I-Mutant3.0 showed reliability, overall accuracy remains moderate, necessitating improved computational methods for mutation analysis.

More Related Videos

Measuring Protein Stability in Living Zebrafish Embryos Using Fluorescence Decay After Photoconversion (FDAP)
09:45

Measuring Protein Stability in Living Zebrafish Embryos Using Fluorescence Decay After Photoconversion (FDAP)

Published on: January 28, 2015

A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

Related Experiment Videos

Last Updated: Jun 15, 2026

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project
07:22

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project

Published on: February 11, 2019

Measuring Protein Stability in Living Zebrafish Embryos Using Fluorescence Decay After Photoconversion (FDAP)
09:45

Measuring Protein Stability in Living Zebrafish Embryos Using Fluorescence Decay After Photoconversion (FDAP)

Published on: January 28, 2015

A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

Area of Science:

  • Biochemistry and Molecular Biology
  • Computational Biology
  • Protein Science

Background:

  • Protein stability is crucial for biomolecular function, activity, and regulation.
  • Mutations altering protein stability are linked to various diseases.
  • Computational tools are essential for predicting stability changes due to mutations.

Purpose of the Study:

  • To systematically analyze and compare the performance of 11 online protein stability prediction tools.
  • To assess predictor accuracy based on mutation location, protein structure type, and biophysical properties.
  • To identify the most reliable computational methods for predicting mutation-induced stability changes.

Main Methods:

  • Evaluated 11 distinct protein stability predictors: CUPSAT, Dmutant, FoldX, I-Mutant2.0, I-Mutant3.0 (sequence and structure versions), MultiMutate, MUpro, SCide, Scpred, and SRide.
  • Utilized a dataset of 1,784 single mutations from 80 proteins, excluding training data.
  • Assessed performance based on mutation location (secondary structures, surface, core), protein structure type, altered residue volumes, and charge interactions.

Main Results:

  • All evaluated programs demonstrated predictions consistent with experimental data.
  • I-Mutant3.0 (structure-based), Dmutant, and FoldX emerged as the most dependable predictors.
  • Stability-centric predictors exhibited comparable accuracy levels.
  • The highest prediction accuracy achieved was approximately 60%.

Conclusions:

  • While several protein stability predictors show promise, their current accuracy is only moderate.
  • Structural information enhances the reliability of predictors like I-Mutant3.0.
  • Development of more accurate computational tools is necessary for routine analysis of mutation effects on protein stability.