What is he best known for?
The fields of study he is best known for:
- Enzyme
- Biochemistry
- Amino acid
His scientific interests lie mostly in Casein, Crystallography, Protein secondary structure, Biochemistry and Molecular model.
His research integrates issues of Amino acid, Fibril and Micelle in his study of Casein.
His Crystallography research includes themes of Ion, Dimer and Intermolecular force.
Harold M. Farrell has included themes like Lactalbumin, Raman spectroscopy, Circular dichroism, Protein structure and Side chain in his Protein secondary structure study.
His Circular dichroism research is multidisciplinary, incorporating perspectives in Polyproline helix, Denaturation, Polymer, Monomer and Conformational change.
His Protein primary structure study combines topics in areas such as Whey protein, Proteolysis, Homology, Acid phosphatase and Serum albumin.
His most cited work include:
- Nomenclature of the Proteins of Cows’ Milk—Sixth Revision (911 citations)
- Nomenclature of Proteins of Cow's Milk: Fifth Revision (712 citations)
- Secondary structural studies of bovine caseins: temperature dependence of β-casein structure as analyzed by circular dichroism and FTIR spectroscopy and correlation with micellization (149 citations)
What are the main themes of his work throughout his whole career to date?
Harold M. Farrell focuses on Casein, Biochemistry, Crystallography, Micelle and Protein secondary structure.
His studies deal with areas such as Calcium, Chromatography, Colloid, Hydrophobic effect and Solubility as well as Casein.
His Crystallography study integrates concerns from other disciplines, such as Molecular model and Infrared spectroscopy.
The study incorporates disciplines such as Relaxation, Molecular dynamics, Virial coefficient and Analytical chemistry in addition to Micelle.
His Protein secondary structure study incorporates themes from Protein structure, Side chain, Peptide sequence and Protein tertiary structure.
While the research belongs to areas of Circular dichroism, he spends his time largely on the problem of Polyproline helix, intersecting his research to questions surrounding Denaturation.
He most often published in these fields:
- Casein (45.05%)
- Biochemistry (32.97%)
- Crystallography (30.77%)
What were the highlights of his more recent work (between 1999-2014)?
- Circular dichroism (16.48%)
- Crystallography (30.77%)
- Protein secondary structure (16.48%)
In recent papers he was focusing on the following fields of study:
The scientist’s investigation covers issues in Circular dichroism, Crystallography, Protein secondary structure, Casein and Polyproline helix.
His studies in Circular dichroism integrate themes in fields like Bioorganic chemistry, Biophysics and Denaturation.
His Crystallography research is multidisciplinary, relying on both Peptide and Molecular dynamics.
His Protein secondary structure research integrates issues from Protein structure, Protein tertiary structure and Protein folding.
His Casein study which covers Monomer that intersects with Ultracentrifuge and Fibril.
Harold M. Farrell works mostly in the field of Polyproline helix, limiting it down to topics relating to Molecular model and, in certain cases, Micelle, as a part of the same area of interest.
Between 1999 and 2014, his most popular works were:
- Secondary structural studies of bovine caseins: temperature dependence of β-casein structure as analyzed by circular dichroism and FTIR spectroscopy and correlation with micellization (149 citations)
- Environmental influences on bovine kappa-casein: reduction and conversion to fibrillar (amyloid) structures. (85 citations)
- Molten globule structures in milk proteins: implications for potential new structure-function relationships. (65 citations)
In his most recent research, the most cited papers focused on:
- Enzyme
- Biochemistry
- Amino acid
Harold M. Farrell mostly deals with Protein secondary structure, Circular dichroism, Crystallography, Conformational change and Denaturation.
Harold M. Farrell interconnects Globular protein and Polymer, Monomer in the investigation of issues within Circular dichroism.
Monomer and Casein are frequently intertwined in his study.
His Conformational change study frequently draws connections to adjacent fields such as Polyproline helix.
His research integrates issues of Biophysics, Lactalbumin and Molecular dynamics in his study of Molten globule.
Amyloid combines with fields such as Protein structure, Biochemistry, Fibril and Ultracentrifuge in his research.
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