George Nemethy mostly deals with Hydrogen bond, Thermodynamics, Stereochemistry, Amino acid and Amino acid residue. His Thermodynamics study frequently links to adjacent areas such as Molecule. George Nemethy has researched Molecule in several fields, including Mole fraction, Physical chemistry and Partition function.
His Stereochemistry research incorporates themes from Polypeptide chain, Alpha-aminoisobutyric acid and Turn. His Amino acid research is multidisciplinary, incorporating elements of Residue and Aminobutyric acid. His Computational chemistry study combines topics from a wide range of disciplines, such as Crystallography, Intramolecular force, Ring and Conformational energy.
Crystallography, Stereochemistry, Hydrogen bond, Molecule and Thermodynamics are his primary areas of study. His work deals with themes such as Protein structure, Side chain, Steric effects and Antiparallel, which intersect with Crystallography. His study on Stereochemistry also encompasses disciplines like
His work carried out in the field of Hydrogen bond brings together such families of science as Amino acid and Random coil. He combines subjects such as Partition function and Physical chemistry with his study of Molecule. His work on Material properties, Enthalpy and Mole fraction as part of general Thermodynamics research is frequently linked to Gramicidin S, bridging the gap between disciplines.
His primary areas of study are Stereochemistry, Crystallography, Conformational energy, Molecule and Hydrogen bond. His studies deal with areas such as Amino acid, Relaxation and Oligopeptide as well as Stereochemistry. His biological study spans a wide range of topics, including Proline, Antiparallel, Phenylalanine and Nuclear magnetic resonance.
His Conformational energy research includes themes of Polypeptide chain, Computational chemistry and Group. The study incorporates disciplines such as Physical chemistry and Thermodynamics in addition to Molecule. George Nemethy integrates many fields in his works, including Hydrogen bond and Monte carlo simulated annealing.
The scientist’s investigation covers issues in Stereochemistry, Amino acid, Hydrogen bond, Amino acid residue and Potential energy. His study on α helices is often connected to Monte carlo simulated annealing as part of broader study in Stereochemistry. His Amino acid study integrates concerns from other disciplines, such as Residue and Aminobutyric acid.
His Hydrogen bond study frequently draws connections between adjacent fields such as Intermolecular potential. George Nemethy works mostly in the field of Computational chemistry, limiting it down to concerns involving Conformational energy and, occasionally, Thermodynamics and Group. His Physical chemistry research is multidisciplinary, relying on both Molecule, Accessible surface area, Heat capacity and Enthalpy.
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.
Structure of Water and Hydrophobic Bonding in Proteins. I. A Model for the Thermodynamic Properties of Liquid Water
George Némethy;Harold A. Scheraga.
Journal of Chemical Physics (1962)
Energy parameters in polypeptides. 9. Updating of geometrical parameters, nonbonded interactions, and hydrogen bond interactions for the naturally occurring amino acids
George Nemethy;Marcia S. Pottle;Harold A. Scheraga.
The Journal of Physical Chemistry (1983)
THE STRUCTURE OF WATER AND HYDROPHOBIC BONDING IN PROTEINS. III. THE THERMODYNAMIC PROPERTIES OF HYDROPHOBIC BONDS IN PROTEINS1,2
George Némethy;Harold A. Scheraga.
The Journal of Physical Chemistry (1962)
Accessible Surface Areas as a Measure of the Thermodynamic Parameters of Hydration of Peptides
Tatsuo Ooi;Motohisa Oobatake;George Nemethy;Harold A. Scheraga.
Proceedings of the National Academy of Sciences of the United States of America (1987)
Conformational Analysis of the 20 Naturally Occurring Amino Acid Residues Using ECEPP
S. Scott Zimmerman;Marcia S. Pottle;George Némethy;Harold A. Scheraga.
Macromolecules (1977)
Structure of Water and Hydrophobic Bonding in Proteins. II. Model for the Thermodynamic Properties of Aqueous Solutions of Hydrocarbons
George Némethy;Harold A. Scheraga.
Journal of Chemical Physics (1962)
Energy parameters in polypeptides. 10. Improved geometrical parameters and nonbonded interactions for use in the ECEPP/3 algorithm, with application to proline-containing peptides
George Nemethy;Kenneth D. Gibson;Kathleen A. Palmer;Chang No. Yoon.
The Journal of Physical Chemistry (1994)
Structure of Water and Hydrophobic Bonding in Proteins. IV. The Thermodynamic Properties of Liquid Deuterium Oxide
George Némethy;Harold A. Scheraga.
Journal of Chemical Physics (1964)
Intermolecular potentials from crystal data. 6. Determination of empirical potentials for O-H...O = C hydrogen bonds from packing configurations
Manfred J. Sippl;George Nemethy;Harold A. Scheraga.
The Journal of Physical Chemistry (1984)
The γ Turn, a Possible Folded Conformation of the Polypeptide Chain. Comparison with the β Turn
George Némethy;Morton P. Printz.
Macromolecules (1972)
If you think any of the details on this page are incorrect, let us know.
We appreciate your kind effort to assist us to improve this page, it would be helpful providing us with as much detail as possible in the text box below:
Cornell University
The Gordon Life Science Institute
Stanford University
Harvard University
Cornell University
University of Naples Federico II
Hungarian Academy of Sciences
University of Michigan–Ann Arbor
University of Pennsylvania
University of North Carolina at Chapel Hill
VMware
Guangdong University of Technology
Georgia Institute of Technology
Tokyo Institute of Technology
Chinese Academy of Sciences
Los Alamos National Laboratory
Federal University of Toulouse Midi-Pyrénées
Leiden University
University of California, San Francisco
University of Oregon
Universidade de São Paulo
Yale University
Karolinska Institute
University of Cape Town
Seoul National University
Brookhaven National Laboratory