Hydrogen exchange kinetics of human hemoglobins. The pH dependence of solvent accessibility in cyanomet-, oxy-, and deoxyhemoglobin.
Open Access
- 1 May 1978
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 253 (10) , 3702-3707
- https://doi.org/10.1016/s0021-9258(17)34858-5
Abstract
No abstract availableThis publication has 19 references indexed in Scilit:
- The structure of horse methaemoglobin at 2.0 Å resolutionJournal of Molecular Biology, 1977
- Dynamics of folded proteinsNature, 1977
- Effect of ligand and heme on conformational stability (intramolecular conformational motility) of hemoglobin as revealed by hydrogen exchangeFEBS Letters, 1977
- The role of bound water in haemoglobin and myoblobinBiosystems, 1977
- Effect of inter‐subunit contact on intramolecular conformational motility (conformational stability) of hemoglobin as revealed by hydrogen exchangeFEBS Letters, 1976
- Hydrogen-tritium exchange kinetics of soybean trypsin inhibitor (Kunitz). Solvent acessibility in the folded conformationBiochemistry, 1975
- A Study by the Hydrogen-Exchange Method of the Complex Formed between the Basic Pancreatic Trypsin Inhibitor and TrypsinEuropean Journal of Biochemistry, 1974
- Effects of ligand binding on the rates of hydrogen exchange in myoglobin and hemoglobinBiochemistry, 1973
- Equilibriums of organic phosphates with horse oxyhemoglobinBiochemistry, 1972
- Molecular aspects of hydrogen-deuterium exchange in macromoleculesJournal of Colloid and Interface Science, 1968