What is he best known for?
The fields of study he is best known for:
- Quantum mechanics
- Enzyme
- Amino acid
His main research concerns Crystallography, Stereochemistry, Protein structure, Molecule and Protein folding.
His study in Crystallography is interdisciplinary in nature, drawing from both Dihedral angle, Hydrogen bond, Side chain and Energy minimization.
His Stereochemistry study which covers Amino acid that intersects with Amino acid residue and Residue.
Harold A. Scheraga interconnects Antiparallel, Potential energy, Binding site and Globular protein in the investigation of issues within Protein structure.
As a part of the same scientific study, Harold A. Scheraga usually deals with the Molecule, concentrating on Computational chemistry and frequently concerns with Energy.
His Protein folding research is multidisciplinary, relying on both Folding, Statistical physics and Molecular dynamics.
His most cited work include:
- Energy parameters in polypeptides. VII. Geometric parameters, partial atomic charges, nonbonded interactions, hydrogen bond interactions, and intrinsic torsional potentials for the naturally occurring amino acids (1357 citations)
- Monte Carlo-minimization approach to the multiple-minima problem in protein folding. (1091 citations)
- Structure of Water and Hydrophobic Bonding in Proteins. I. A Model for the Thermodynamic Properties of Liquid Water (921 citations)
What are the main themes of his work throughout his whole career to date?
Harold A. Scheraga focuses on Crystallography, Stereochemistry, Protein structure, Molecule and Protein folding.
Harold A. Scheraga combines subjects such as Dihedral angle, Hydrogen bond and Side chain with his study of Crystallography.
In his research on the topic of Stereochemistry, Thrombin is strongly related with Biochemistry.
In his work, Statistical physics is strongly intertwined with Force field, which is a subfield of Protein structure.
His Molecule research integrates issues from Chemical physics, Computational chemistry and Thermodynamics.
As a member of one scientific family, he mostly works in the field of Protein folding, focusing on Bovine pancreatic ribonuclease and, on occasion, Oxidative folding.
He most often published in these fields:
- Crystallography (31.38%)
- Stereochemistry (23.31%)
- Protein structure (17.96%)
What were the highlights of his more recent work (between 2006-2021)?
- Crystallography (31.38%)
- Molecular dynamics (7.17%)
- Protein structure (17.96%)
In recent papers he was focusing on the following fields of study:
His primary areas of study are Crystallography, Molecular dynamics, Protein structure, Protein folding and Force field.
His research investigates the connection between Crystallography and topics such as Peptide that intersect with problems in Stereochemistry.
He has researched Molecular dynamics in several fields, including Chemical physics, Side chain, Biophysics and Molecule.
His Protein structure study incorporates themes from Conformational isomerism, Crystal structure, Hydrogen bond and Chemical shift.
He studied Protein folding and Folding that intersect with Oxidative folding and Bovine pancreatic ribonuclease.
His Force field study integrates concerns from other disciplines, such as Mesoscopic physics, Ab initio, Statistical physics, Biological system and Principal component analysis.
Between 2006 and 2021, his most popular works were:
- Significant progress in predicting the crystal structures of small organic molecules--a report on the fourth blind test. (318 citations)
- Protein-Folding Dynamics: Overview of Molecular Simulation Techniques (286 citations)
- Towards crystal structure prediction of complex organic compounds – a report on the fifth blind test (281 citations)
In his most recent research, the most cited papers focused on:
- Quantum mechanics
- Enzyme
- Amino acid
Harold A. Scheraga mainly investigates Molecular dynamics, Crystallography, Protein structure, Force field and Protein folding.
The Molecular dynamics study combines topics in areas such as Chemical physics, Hydrophobic effect and Molecule.
Harold A. Scheraga is interested in Crystal structure, which is a field of Crystallography.
Harold A. Scheraga has researched Protein structure in several fields, including Side chain, Fourier series, Monomer and Chemical shift.
His Side chain study integrates concerns from other disciplines, such as Amino acid, Conformational isomerism, Maxima and minima and Thermodynamics.
His research in Protein folding intersects with topics in Statistical physics and Principal component analysis.
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.
