What is he best known for?
The fields of study he is best known for:
Patrick Argos mainly investigates Protein structure, Peptide sequence, Crystallography, Amino acid and Genetics.
His Protein structure research integrates issues from Globin, Algorithm, Protein tertiary structure and Protein folding.
His Peptide sequence study is focused on Biochemistry in general.
His Crystallography study combines topics in areas such as Thermostability, Protein secondary structure, Bacteriorhodopsin, Hydrogen bond and Thermal stability.
His work carried out in the field of Amino acid brings together such families of science as Sequence alignment, Residue, Stereochemistry, Ferredoxin and Membrane protein.
His study in the field of Gene, Mosaic virus, Plant virus and DNA polymerase is also linked to topics like Klenow fragment.
His most cited work include:
- Knowledge-based protein secondary structure assignment. (1884 citations)
- Primary structural comparison of RNA-dependent polymerases from plant, animal and bacterial viruses. (715 citations)
- Protein thermal stability, hydrogen bonds, and ion pairs (577 citations)
What are the main themes of his work throughout his whole career to date?
Patrick Argos focuses on Crystallography, Protein structure, Protein secondary structure, Amino acid and Biochemistry.
His work deals with themes such as Dihedral angle, Hydrogen bond, Protein subunit and Polar, which intersect with Crystallography.
His work in Protein structure covers topics such as Protein folding which are related to areas like Folding.
Patrick Argos combines subjects such as Chou–Fasman method and Protein Data Bank with his study of Protein secondary structure.
His Amino acid research is multidisciplinary, relying on both Residue and Ferredoxin.
His work is dedicated to discovering how Biochemistry, Stereochemistry are connected with Nicotinamide, Dehydrogenase and Helix and other disciplines.
He most often published in these fields:
- Crystallography (30.77%)
- Protein structure (28.40%)
- Protein secondary structure (17.75%)
What were the highlights of his more recent work (between 1994-2009)?
- Crystallography (30.77%)
- Protein structure (28.40%)
- Protein folding (15.38%)
In recent papers he was focusing on the following fields of study:
His primary areas of investigation include Crystallography, Protein structure, Protein folding, Protein structure prediction and Amino acid.
The concepts of his Crystallography study are interwoven with issues in Algorithm, Protein engineering and Protein secondary structure.
Patrick Argos applies his multidisciplinary studies on Protein structure and Ligand in his research.
His Protein folding research incorporates elements of Folding, Solvation, Protein tertiary structure and Hydrogen bond.
His Protein structure prediction research is multidisciplinary, incorporating perspectives in Homology modeling, Biological system, Protein sequencing and Threading.
His study explores the link between Amino acid and topics such as Protein Data Bank that cross with problems in Test set and Combinatorics.
Between 1994 and 2009, his most popular works were:
- Knowledge-based protein secondary structure assignment. (1884 citations)
- Protein thermal stability, hydrogen bonds, and ion pairs (577 citations)
- The double cubic lattice method: Efficient approaches to numerical integration of surface area and volume and to dot surface contouring of molecular assemblies (538 citations)
In his most recent research, the most cited papers focused on:
Crystallography, Protein structure, Protein structure prediction, Protein folding and Peptide sequence are his primary areas of study.
Patrick Argos has researched Crystallography in several fields, including Macromolecular Substances, Macromolecule, Algorithm and Crystallization.
Patrick Argos interconnects Helix, Protein secondary structure and Torsional angle in the investigation of issues within Protein structure.
His study in Protein structure prediction is interdisciplinary in nature, drawing from both Homology modeling, Protein tertiary structure, Multiple sequence alignment and Structural alignment.
His Protein folding study combines topics from a wide range of disciplines, such as Thermostability, Hydrogen bond, Thermal stability, Translation and Ribosome.
His Peptide sequence research includes themes of Amino acid and Membrane protein.
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.
