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

Identification of Thermostabilizing Mutations for Membrane Proteins: Rapid Method Based on Statistical Thermodynamics.

The journal of physical chemistry. B - 28 Apr 2016

Yasuda Satoshi, Kajiwara Yuta, Takamuku Yuuki, Suzuki Nanao, Murata Takeshi, Kinoshita Masahiro

Abstract excerpt

Membrane proteins are responsible for the communication between cells and their environments. They are indispensable to the expression of life phenomena and also implicated in a number of diseases. Nevertheless, the studies on membrane proteins are far behind those on water-soluble proteins, primarily due to their low structural stability. Introduction of mutations can enhance their thermostability and stability...

Read the complete abstract on PubMed

Topics

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

Share to Membrane Proteins
Share to Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Conformation

Share to Protein Stability

Share to Thermodynamics

Source

Identifiers

PMID: 27056055
DOI: 10.1021/acs.jpcb.6b01405

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of Thermostabilizing Mutations for Membrane Proteins: Rapid Method Based on Statistical Thermodynamics.PMID 27056055Read ↗

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

Physical Origin of Thermostabilization by a Quadruple Mutation for the Adenosine A2a Receptor in the Active State.Semantic proximity Read ↗

Accurate and Rigorous Prediction of the Changes in Protein Free Energies in a Large-Scale Mutation Scan.Semantic proximity Read ↗

Methodology for Further Thermostabilization of an Intrinsically Thermostable Membrane Protein Using Amino Acid Mutations with Its Original Function Being Retained.Semantic proximity Read ↗

MPTherm-pred: Analysis and Prediction of Thermal Stability Changes upon Mutations in Transmembrane Proteins.Semantic proximity Read ↗

Hot-Spot Residues to be Mutated Common in G Protein-Coupled Receptors of Class A: Identification of Thermostabilizing Mutations Followed by Determination of Three-Dimensional Structures for Two Example Receptors.Semantic proximity Read ↗

A methodology for creating mutants of G-protein coupled receptors stabilized in active state by combining statistical thermodynamics and evolutionary molecular engineering.Semantic proximity Read ↗

Identifying Thermostabilizing Mutations in Membrane Proteins by Bioinformatics.Semantic proximity Read ↗

Dynamic behavior of the active and inactive states of the adenosine A(2A) receptor.Semantic proximity Read ↗

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

Protein thermostability calculations using alchemical free energy simulations.Semantic proximity Read ↗

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

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