Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

An efficient method to predict protein thermostability in alanine mutation.

Physical chemistry chemical physics : PCCP - 14 Dec 2022

Gao Ya, Wang Bo, Hu Shiyu, Zhu Tong, Zhang John Z H

Abstract excerpt

The relationship between protein sequence and its thermodynamic stability is a critical aspect of computational protein design. In this work, we present a new theoretical method to calculate the free energy change (ΔΔG) resulting from a single-point amino acid mutation to alanine in a protein sequence. The method is derived based on physical interactions and is very efficient in estimating the free energy changes...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alanine
Share to Amino Acid Sequence
Share to Mutation

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Proteins

Share to Thermodynamics

Source

Identifiers

PMID: 36449314
DOI: 10.1039/d2cp04236c

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

An efficient method to predict protein thermostability in alanine mutation.PMID 36449314Read ↗

Computational evaluation of protein stability change upon mutations.Semantic proximity Read ↗

Identification of thermostabilizing mutations for a membrane protein whose three-dimensional structure is unknown.Semantic proximity Read ↗

Role of simple descriptors and applicability domain in predicting change in protein thermostability.Semantic proximity Read ↗

Relative importance of secondary structure and solvent accessibility to the stability of protein mutants. A case study with amino acid properties and energetics on T4 and human lysozymes.Semantic proximity Read ↗

Simulation analysis of selective alanine mutation effect on stability of human prion protein.Semantic proximity Read ↗

Increasing protein conformational stability by optimizing beta-turn sequence.Semantic proximity Read ↗

Protein stability prediction: a Poisson-Boltzmann approach.Semantic proximity Read ↗

A rapid, ensemble and free energy based method for engineering protein stabilities.Semantic proximity Read ↗

Performance of Web tools for predicting changes in protein stability caused by mutations.Semantic proximity Read ↗

Accurate Prediction of Protein Thermodynamic Stability Changes upon Residue Mutation using Free Energy Perturbation.Semantic proximity Read ↗

Target-template relationships in protein structure prediction and their effect on the accuracy of thermostability calculations.Semantic proximity Read ↗

Robust folding of a de novo designed ideal protein even with most of the core mutated to valine.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.