What is he best known for?
The fields of study he is best known for:
- Quantum mechanics
- Enzyme
- Gene
Martin Karplus focuses on Molecular dynamics, Crystallography, Protein structure, Computational chemistry and Chemical physics.
The various areas that Martin Karplus examines in his Molecular dynamics study include Dihedral angle, Hydrogen bond, Helix, Native state and Implicit solvation.
His study looks at the intersection of Crystallography and topics like Crambin with Crystal structure.
His Protein structure research includes elements of Protein secondary structure, Protein folding, Structural biology and Nuclear magnetic resonance spectroscopy, Stereochemistry.
His work deals with themes such as Solvent models, Dipole, Thermodynamics, Molecule and Monomer, which intersect with Computational chemistry.
His Thermodynamics study also includes fields such as
- Solvation, which have a strong connection to Interaction energy and Potential of mean force,
- Force field and related Ab initio.
His most cited work include:
- CHARMM: A program for macromolecular energy, minimization, and dynamics calculations (12059 citations)
- All-atom empirical potential for molecular modeling and dynamics studies of proteins. (10375 citations)
- All-atom empirical potential for molecular modeling and dynamics studies of proteins. (10375 citations)
What are the main themes of his work throughout his whole career to date?
His primary areas of investigation include Molecular dynamics, Crystallography, Computational chemistry, Stereochemistry and Chemical physics.
His Molecular dynamics research integrates issues from Biophysics, Thermodynamics, Molecule, Hydrogen bond and Statistical physics.
Martin Karplus studied Molecule and Atomic physics that intersect with Electron.
His Crystallography research is multidisciplinary, incorporating perspectives in Protein structure, Nuclear magnetic resonance spectroscopy and Protein folding.
His Protein folding study integrates concerns from other disciplines, such as Folding and Native state.
His Computational chemistry study combines topics from a wide range of disciplines, such as Solvation, Ab initio and Molecular physics.
He most often published in these fields:
- Molecular dynamics (32.93%)
- Crystallography (22.54%)
- Computational chemistry (18.16%)
What were the highlights of his more recent work (between 2005-2021)?
- Molecular dynamics (32.93%)
- Statistical physics (13.79%)
- Biophysics (9.52%)
In recent papers he was focusing on the following fields of study:
Martin Karplus mainly focuses on Molecular dynamics, Statistical physics, Biophysics, Crystallography and Protein structure.
Molecular dynamics is a subfield of Computational chemistry that Martin Karplus studies.
His studies in Statistical physics integrate themes in fields like Hemoglobin, Non-equilibrium thermodynamics and Energy.
His work carried out in the field of Biophysics brings together such families of science as Kinesin, Biochemistry, Adenosine triphosphate, Binding site and Function.
His Crystallography research also works with subjects such as
- Protein folding which intersects with area such as Native state,
- Plasma protein binding that connect with fields like Interaction energy,
- Solvation most often made with reference to Chemical physics.
His Protein structure research includes themes of Stereochemistry and Allosteric regulation.
Between 2005 and 2021, his most popular works were:
- CHARMM: the biomolecular simulation program. (4881 citations)
- CHARMM: the biomolecular simulation program. (4881 citations)
- A hierarchy of timescales in protein dynamics is linked to enzyme catalysis. (785 citations)
In his most recent research, the most cited papers focused on:
- Quantum mechanics
- Enzyme
- Gene
Martin Karplus mainly investigates Molecular dynamics, Protein structure, Computational chemistry, Biophysics and Crystallography.
His Molecular dynamics study incorporates themes from Chemical physics, Statistical physics, Interaction energy and Function.
His research in Protein structure intersects with topics in Protozoan Proteins, Protein subunit, Conformational change, Stereochemistry and Implicit solvation.
In the field of Computational chemistry, his study on Drude particle overlaps with subjects such as Mechanical force.
Martin Karplus combines subjects such as Plasma protein binding, Biochemistry, Binding site, Actin and Bundle with his study of Biophysics.
His Crystallography research includes elements of Myosin, Kinesin, Mutant and Protein folding.
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.
