Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Mutations

Mutations

Mutations

Mutations

Mutations are changes in the sequence of DNA. These changes can occur spontaneously or they can be induced by exposure to environmental factors. Mutations can be characterized in a number of different ways: whether and how they alter the amino acid sequence of the protein, whether they occur over a small or large area of DNA, and whether they occur in somatic cells or germline cells.
Chromosomal Alterations Are Large-Scale Mutations
While point mutations are changes in a single nucleotide in...

Cancers Originate from Somatic Mutations in a Single Cell

Cancers Originate from Somatic Mutations in a Single Cell

Cancer arises from mutations in the critical genes that allow healthy cells to escape cell cycle regulation and acquire the ability to proliferate indefinitely. Though originating from a single mutation event in one of the originator cells, cancer progresses when the mutant cell lines continue to gain more and more mutations, and finally, become malignant. For example, chronic myelogenous leukemia (CML) develops initially as a non-lethal increase in white blood cells, which progressively...

Viral Mutations

Viral Mutations

A mutation is a change in the sequence of bases of DNA or RNA in a genome. Some mutations occur during replication of the genome due to errors made by the polymerase enzymes that replicate DNA or RNA. Unlike DNA polymerase, RNA polymerase is prone to errors because it is not capable of “proofreading” its work. Viruses with RNA-based genomes, like HIV, therefore accrue mutations faster than viruses with DNA-based genomes. Because mutation and recombination provide the raw material...

What is Genetic Engineering?

What is Genetic Engineering?

Mutation, Gene Flow, and Genetic Drift

Mutation, Gene Flow, and Genetic Drift

In a population that is not at Hardy-Weinberg equilibrium, the frequency of alleles changes over time. Therefore, any deviations from the five conditions of Hardy-Weinberg equilibrium can alter the genetic variation of a given population. Conditions that change the genetic variability of a population include mutations, natural selection, non-random mating, gene flow, and genetic drift (small population size).

You might also read

Related Articles

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

Sort by

Same author

Development of a pKa predictor (pKaLearn) by leveraging teaching experience to improve machine learning.

Communications chemistry·2026

Same author

Integration of computational and experimental techniques for the discovery of PL<sup>pro</sup> covalent inhibitors. When large virtual screening and rational design meet.

European journal of medicinal chemistry·2026

Same author

α-Ketoamides-based covalent inhibitors in drug discovery: Current status and synthetic methods.

European journal of medicinal chemistry·2026

Same author

Inhibitor-induced dimerization mediates lufotrelvir resistance in mutants of SARS-CoV-2 3C-like protease.

Protein science : a publication of the Protein Society·2025

Same author

Mechanistic Characterization of Covalent Enzyme Inhibition by Isothermal Titration Calorimetry Kinetic Competition (ITC-KC).

Analytical chemistry·2025

Same author

A sensitive and scalable fluorescence anisotropy single stranded RNA targeting approach for monitoring riboswitch conformational states.

Nucleic acids research·2024

Search research articles

Related Experiment Video

Updated: Feb 15, 2026

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

Single-Point Mutation with a Rotamer Library Toolkit: Toward Protein Engineering.

Joshua Pottel¹, Nicolas Moitessier¹

¹Department of Chemistry, McGill University , 801 Sherbrooke Street West, Montreal, QC, Canada H3A 0B8.

Journal of Chemical Information and Modeling

|December 2, 2015

Summary

Computational tools predict protein side-chain conformations for enhanced biocatalyst engineering. This approach optimizes enzyme function and improves protein-ligand docking accuracy, advancing protein engineering applications.

More Related Videos

A Protocol for Functional Assessment of Whole-Protein Saturation Mutagenesis Libraries Utilizing High-Throughput Sequencing

A Protocol for Functional Assessment of Whole-Protein Saturation Mutagenesis Libraries Utilizing High-Throughput Sequencing

Published on: July 3, 2016

Combinatorial Synthesis of and High-throughput Protein Release from Polymer Film and Nanoparticle Libraries

Combinatorial Synthesis of and High-throughput Protein Release from Polymer Film and Nanoparticle Libraries

Published on: September 6, 2012

Related Experiment Videos

Last Updated: Feb 15, 2026

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

A Protocol for Functional Assessment of Whole-Protein Saturation Mutagenesis Libraries Utilizing High-Throughput Sequencing

A Protocol for Functional Assessment of Whole-Protein Saturation Mutagenesis Libraries Utilizing High-Throughput Sequencing

Published on: July 3, 2016

Combinatorial Synthesis of and High-throughput Protein Release from Polymer Film and Nanoparticle Libraries

Combinatorial Synthesis of and High-throughput Protein Release from Polymer Film and Nanoparticle Libraries

Published on: September 6, 2012

Area of Science:

Computational biology
Protein engineering
Biocatalysis

Background:

Enzymes offer high selectivity for chemical reactions.
Protein engineering aims to expand enzyme capabilities beyond natural functions.
Computational methods are crucial for handling the complexity of protein mutations.

Purpose of the Study:

To develop automated computational tools for predicting protein side-chain conformations after mutation.
To create versatile conformational libraries for amino acids.
To assess the impact of side-chain prediction on protein-ligand docking.

Main Methods:

Combined molecular mechanics and statistical data for conformation prediction.
Developed automated tools to extract protein structural information.
Created amino acid-specific and kinase-family-specific conformational libraries.
Applied mutation protocols to self- and cross-docking benchmarks.

Main Results:

Achieved average root-mean-square deviations (RMSDs) of 0.91 and 1.01 Å for side-chain conformation prediction.
Kinase-specific libraries improved RMSD by 2%, while residue-specific libraries improved it by 17%.
Side-chain reconstruction minimally impacted docking accuracy (approx. 2% difference in RMSD cutoff).

Conclusions:

The developed computational tools accurately predict protein side-chain conformations.
Optimized conformational libraries enhance prediction accuracy, especially for specific protein families like kinases.
The side-chain reconstruction protocol is compatible with docking software, showing minimal negative effects on accuracy.