Unfolding and Hydrogen Exchange of Proteins: the Three-dimensional Ising Lattice as a Model
- 1 October 1969
- journal article
- Published by Springer Nature in Nature
- Vol. 224 (5215) , 175-177
- https://doi.org/10.1038/224175a0
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- Reversible Denaturation of Sperm Whale Myoglobin. II. Thermodynamic AnalysisJournal of the American Chemical Society, 1967
- Validity of the “two‐state” hypothesis for conformational transitions of proteinsBiopolymers, 1966
- Equilibrium and kinetics of the unfolding of lysozyme (muramidase) by guanidine hydrochlorideJournal of Molecular Biology, 1966
- The Thermodynamics of Protein Denaturation. I. The Denaturation of ChymotrypsinogenJournal of the American Chemical Society, 1964
- Theory of the Phase Transition between Helix and Random Coil in Polypeptide ChainsThe Journal of Chemical Physics, 1959
- On a Model for Helix-Random Coil Transition in Polypeptides I. The Model and its Thermal Behavior.The Journal of Physical Chemistry, 1959
- Generalization of the One-Dimensional Ising Model Applicable to Helix Transitions in Nucleic Acids and ProteinsThe Journal of Chemical Physics, 1959
- Statistical Mechanics of Helix-Coil Transitions in Biological MacromoleculesThe Journal of Chemical Physics, 1959
- Exchange of hydrogen atoms in insulin with deuterium atoms in aqueous solutionsBiochimica et Biophysica Acta, 1954
- Beitrag zur Theorie des FerromagnetismusZeitschrift für Physik, 1925