What is he best known for?
The fields of study he is best known for:
His main research concerns Antifreeze protein, Ice binding, Biochemistry, Crystallography and Biophysics.
Peter L. Davies integrates many fields in his works, including Antifreeze protein and Ice crystals.
His biological study spans a wide range of topics, including Threonine, Hydrogen bond and Protein folding.
His Crystallography study integrates concerns from other disciplines, such as Antiparallel, Nuclear magnetic resonance spectroscopy, Mineralogy and Clathrate hydrate.
His Calpain research is multidisciplinary, incorporating elements of Proteases, Protein subunit and Active site.
His Amino acid research is multidisciplinary, relying on both Stereochemistry and Peptide.
His most cited work include:
- Antifreeze proteins of teleost fishes. (388 citations)
- Biochemistry of fish antifreeze proteins. (356 citations)
- β-Helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect (335 citations)
What are the main themes of his work throughout his whole career to date?
Peter L. Davies spends much of his time researching Antifreeze protein, Biochemistry, Ice binding, Biophysics and Crystallography.
His Antifreeze protein research incorporates themes from Protein structure, Molecular biology, Gene and Antifreeze.
His studies deal with areas such as Plasma protein binding and Binding site as well as Protein structure.
In his research on the topic of Ice binding, Peptide is strongly related with Stereochemistry.
His Biophysics study integrates concerns from other disciplines, such as Bacterial adhesin, Microfluidics and Bacteria.
His Crystallography research includes themes of Crystallization and Molecule.
He most often published in these fields:
- Antifreeze protein (63.80%)
- Biochemistry (39.88%)
- Ice binding (27.91%)
What were the highlights of his more recent work (between 2016-2021)?
- Antifreeze protein (63.80%)
- Biophysics (19.63%)
- Bacterial adhesin (4.91%)
In recent papers he was focusing on the following fields of study:
His main research concerns Antifreeze protein, Biophysics, Bacterial adhesin, Ice binding and Biofilm.
His biological study spans a wide range of topics, including Crystallography, Gene isoform and Antifreeze.
His Biophysics research is multidisciplinary, incorporating elements of Protein structure, Calpain, Protease and Proteases.
His Bacterial adhesin research is within the category of Biochemistry.
Peter L. Davies has researched Ice binding in several fields, including Astrobiology, Ecology and Growth control.
His study explores the link between Biofilm and topics such as Vibrio cholerae that cross with problems in Peptide, Hemagglutination, Cholera and Colonization.
Between 2016 and 2021, his most popular works were:
- Structure of a 1.5-MDa adhesin that binds its Antarctic bacterium to diatoms and ice (48 citations)
- An ice-binding and tandem beta-sandwich domain-containing protein in Shewanella frigidimarina is a potential new type of ice adhesin. (25 citations)
- RTX Adhesins are Key Bacterial Surface Megaproteins in the Formation of Biofilms (22 citations)
In his most recent research, the most cited papers focused on:
Peter L. Davies spends much of his time researching Antifreeze protein, Biophysics, Bacterial adhesin, Protein structure and Ice binding.
His Antifreeze protein study is related to the wider topic of Biochemistry.
Many of his research projects under Biochemistry are closely connected to Intein with Intein, tying the diverse disciplines of science together.
His research integrates issues of Protease inhibitor and Leupeptin in his study of Biophysics.
His Bacterial adhesin research also works with subjects such as
- Biofilm most often made with reference to Secretion,
- Bacterial outer membrane that intertwine with fields like Periplasmic space and Cell biology.
His Protein structure research includes elements of Fucose, Stereochemistry, Isothermal titration calorimetry and Binding site.
This overview was generated by a machine learning system which analysed the scientist’s
body of work. If you have any feedback, you can
contact us
here.
