Structural and Mutational Analysis of Affinity-Inert Contact Residues at the Growth Hormone−Receptor Interface
- 1 January 1996
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 35 (32), 10300-10307
- https://doi.org/10.1021/bi960513b
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- A Direct Measure of the Contribution of Solvent Reorganization to the Enthalpy of BindingJournal of the American Chemical Society, 1994
- The Crystal Structure of Affinity-matured Human Growth Hormone at 2 Å ResolutionJournal of Molecular Biology, 1994
- Comparison of a Structural and a Functional EpitopeJournal of Molecular Biology, 1993
- Affinity Maturation of Human Growth Hormone by Monovalent Phage DisplayJournal of Molecular Biology, 1993
- Crystals of Human Growth Hormone-Receptor Complexes: Extracellular Domains of the Growth Hormone and Prolactin Receptors and a Hormone Mutant Designed to Prevent Receptor DimerizationJournal of Molecular Biology, 1993
- Solid model compounds and the thermodynamics of protein unfoldingJournal of Molecular Biology, 1991
- Heat capacity of proteinsJournal of Molecular Biology, 1990
- Thermodynamics of dissolution of solid cyclic dipeptides containing hydrophobic side groupsThe Journal of Chemical Thermodynamics, 1989
- The MIDAS display systemJournal of Molecular Graphics, 1988
- A graphics model building and refinement system for macromoleculesJournal of Applied Crystallography, 1978