The Chemical Nature of Hydrogen Bonding in Proteins via NMR: J-Couplings, Chemical Shifts, and AIM Theory
- 1 December 2000
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 122 (51), 12835-12841
- https://doi.org/10.1021/ja0025705
Abstract
No abstract availableThis publication has 42 references indexed in Scilit:
- The Protein Data BankNucleic Acids Research, 2000
- The Role of Polarization and Charge Transfer in the Solvation of BiomoleculesJournal of the American Chemical Society, 1999
- Fast Experiments for Charge-Density Determination: Topological Analysis and Electrostatic Potential of the Amino AcidsL-Asn,dl-Glu,dl-Ser, andL-ThrAngewandte Chemie International Edition, 1999
- Experimental Charge Densities and Intermolecular Interactions: Electrostatic and Topological Analysis of dl-HistidineJournal of the American Chemical Society, 1999
- Assessment of Stability Differences in the Protein G B1 and B2 Domains From Hydrogen-Deuterium Exchange: Comparison with Calorimetric DataBiochemistry, 1995
- p34 cdc2 and ApoptosisScience, 1995
- Low-Barrier Hydrogen Bonds and Enzymic CatalysisScience, 1994
- An analysis of the hydrogen bond in BASE-HF complexes using the theory of atoms in moleculesMolecular Physics, 1988
- Structures des deux formes cristallines de l'acide azélaïque, COOH[CH2]7COOHActa Crystallographica, 1967
- The crystal structure of potassium acid phthalate, KC6H4COOH.COOActa Crystallographica, 1965