Hapten-induced allosteric transition in the light chain dimer of an immunoglobulin
- 1 October 1977
- journal article
- Published by Springer Nature in Nature
- Vol. 269 (5631), 827-829
- https://doi.org/10.1038/269827a0
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- Studies on the three-dimensional structure of immunoglobulinsProgress in Biophysics and Molecular Biology, 1978
- Thermodynamic and spectroscopic comparison of the binding sites of the mouse myeloma protein 315 and of its light chain dimerFEBS Letters, 1977
- On the Structure of the T-cell Receptor for AntigenCold Spring Harbor Symposia on Quantitative Biology, 1977
- Crystallographic structure studies of an IgG molecule and an Fc fragmentNature, 1976
- Two Different VH Gene Products Make Up the T‐Cell ReceptorsScandinavian Journal of Immunology, 1976
- Rotational allomerism and divergent evolution of domains in immunoglobulin light chainsBiochemistry, 1975
- Cooperativity in associating proteins. Monomer-dimer equilibrium coupled to ligand bindingBiochemistry, 1974
- Binding of 2,4-dinitrophenyl compounds and other small molecules to a crystalline .lambda.-type Bence-Jones dimerBiochemistry, 1974
- Hapten stabilization of antibody conformationBiochemistry, 1970
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965