What is he best known for?
The fields of study he is best known for:
Alan R. Fersht spends much of his time researching Crystallography, Barnase, Protein structure, Protein folding and Mutant.
His study in Crystallography is interdisciplinary in nature, drawing from both Folding, Barstar, Chemical physics and Dissociation constant.
The concepts of his Barnase study are interwoven with issues in Protein engineering, Helix, Hydrogen bond and Stereochemistry.
His studies deal with areas such as Valine, C-terminus, Dimer, Computational biology and Tetramer as well as Protein structure.
His research integrates issues of Transition state, Protein secondary structure and Thermodynamics in his study of Protein folding.
His Mutant research includes elements of Suppressor, DNA and DNA-binding protein.
His most cited work include:
- The Structure of the Transition State for Folding of Chymotrypsin Inhibitor 2 Analysed by Protein Engineering Methods: Evidence for a Nucleation-condensation Mechanism for Protein Folding (661 citations)
- The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. (357 citations)
- Strength and co-operativity of contributions of surface salt bridges to protein stability (346 citations)
What are the main themes of his work throughout his whole career to date?
Crystallography, Protein folding, Barnase, Biochemistry and Stereochemistry are his primary areas of study.
His Crystallography research incorporates themes from Folding, Barstar and Denaturation.
His Protein folding study integrates concerns from other disciplines, such as Protein structure, Biophysics, Protein engineering and Protein secondary structure.
His research in Barnase focuses on subjects like Nuclear magnetic resonance spectroscopy, which are connected to Two-dimensional nuclear magnetic resonance spectroscopy.
Alan R. Fersht has included themes like Site-directed mutagenesis, Enzyme, Active site, Chymotrypsin and Hydrogen bond in his Stereochemistry study.
In his study, which falls under the umbrella issue of Mutant, Plasma protein binding is strongly linked to DNA.
He most often published in these fields:
- Crystallography (38.40%)
- Protein folding (34.66%)
- Barnase (27.93%)
What were the highlights of his more recent work (between 2004-2014)?
- Protein folding (34.66%)
- Crystallography (38.40%)
- Biochemistry (25.44%)
In recent papers he was focusing on the following fields of study:
His main research concerns Protein folding, Crystallography, Biochemistry, Mutant and Phi value analysis.
His Protein folding study incorporates themes from Chemical physics, Molecular dynamics, Circular dichroism, Folding and Native state.
His Crystallography research incorporates elements of Biophysics, Protein subunit and Downhill folding.
Alan R. Fersht has researched Phi value analysis in several fields, including Nucleus, Denaturation and Molten globule.
In Protein structure, he works on issues like Stereochemistry, which are connected to Zinc finger.
The study incorporates disciplines such as Barnase and Protein secondary structure in addition to Helix.
Between 2004 and 2014, his most popular works were:
- The crystal structure of human CD1d with and without alpha-galactosylceramide. (333 citations)
- A transient and low-populated protein-folding intermediate at atomic resolution. (229 citations)
- Solution structure of a protein denatured state and folding intermediate. (215 citations)
In his most recent research, the most cited papers focused on:
Alan R. Fersht mainly focuses on Biochemistry, Plasma protein binding, Protein structure, Binding domain and Crystallography.
The various areas that he examines in his Biochemistry study include Biophysics and Stereochemistry.
His Plasma protein binding research is multidisciplinary, incorporating perspectives in Peptide sequence and DNA.
Many of his studies on Protein structure apply to Protein folding as well.
Alan R. Fersht combines subjects such as Folding and Molecular dynamics with his study of Protein folding.
His research in Crystallography intersects with topics in Chemical physics, Denaturation, Nuclear magnetic resonance spectroscopy, Phi value analysis and Chemical shift.
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