ArticleProtein science : a publication of the Protein Society2012
Structural differences between thermophilic and mesophilic membrane proteins.
Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 55 citations in OpenAlex.
- Genomic, Proteomic, and Structural Insights Into the Transition of FtsZ From Thermophiles to Mesophiles Across the Prokaryotic Kingdom.Proteins · 2026Article
- Molecular Adaptations of Thermophilic Proteins-From Mechanistic Understanding to Machine Learning Approaches.ChemistryOpen · 2026Review
- Centromeres in the thermotolerant yeast K. marxianus mediate attachment to a single microtubule.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025Article
- Architecture of native kinetochores revealed by structural studies utilizing a thermophilic yeast.Current biology : CB · 2024Article
- Extremophiles and their expanding biotechnological applications.Archives of microbiology · 2024Review
- Architecture and flexibility of native kinetochores revealed by structural studies utilizing a thermophilic yeast.bioRxiv : the preprint server for biology · 2024Article
- A scalable overexpression of a thermostable recombinant poly-histidine tag carboxyl esterase under lambda promoter: purification, characterization, and protein modelling.Journal, genetic engineering & biotechnology · 2023Article
- StringentJournal of nematology · 2023Article
- Structure of a dimeric photosystem II complex from a cyanobacterium acclimated to far-red light.The Journal of biological chemistry · 2023Article
- High-resolution cryo-electron microscopy structure of photosystem II from the mesophilic cyanobacterium,Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Complete genome of the thermophilic purple sulfur Bacterium Thermochromatium tepidum compared to Allochromatium vinosum and other Chromatiaceae.Photosynthesis research · 2022Article
- iThermo: A Sequence-Based Model for Identifying Thermophilic Proteins Using a Multi-Feature Fusion Strategy.Frontiers in microbiology · 2022Article
- Voronoia 4-ever.Nucleic acids research · 2021Article
- Article
- Building a tRNA thermometer to estimate microbial adaptation to temperature.Nucleic acids research · 2020Article
- A Method for Prediction of Thermophilic Protein Based on Reduced Amino Acids and Mixed Features.Frontiers in bioengineering and biotechnology · 2020Article
- Thermophiles; or, the Modern Prometheus: The Importance of Extreme Microorganisms for Understanding and Applying Extracellular Electron Transfer.Frontiers in microbiology · 2019Article
- Thermophilic Proteins as Versatile Scaffolds for Protein Engineering.Microorganisms · 2018Review
- Accurate computational design of multipass transmembrane proteins.Science (New York, N.Y.) · 2018Article
- Survival and Energy Producing Strategies of Alkane Degraders Under Extreme Conditions and Their Biotechnological Potential.Frontiers in microbiology · 2018Review
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The evolutionary adaptations of thermophilic water-soluble proteins required for maintaining stability at high temperature have been extensively investigated. Little is known about the adaptations in membrane proteins, however. Here, we compare many properties of mesophilic and thermophilic membrane protein structures, including side-chain burial, packing, hydrogen bonding, transmembrane kinks, loop lengths, hydrophobicity, and other sequence features. Most of these properties are quite similar between mesophiles and thermophiles although we observe a slight increase in side-chain burial and possibly a slight decrease in the frequency of transmembrane kinks in thermophilic membrane protein structures. The most striking difference is the increased hydrophobicity of thermophilic transmembrane helices, possibly reflecting more stringent hydrophobicity requirements for membrane partitioning at high temperature. In agreement with prior work examining transmembrane sequences, we find that thermophiles have an increase in small residues (Gly, Ala, Ser, and Val) and a strong suppression of Cys. We also find a relative dearth of most strongly polar residues (Asp, Asn, Glu, Gln, and Arg). These results suggest that in thermophiles, there is significant evolutionary pressure to offload destabilizing polar amino acids, to decrease the entropy cost of side chain burial, and to eliminate thermally sensitive amino acids.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.