Functional analysis of hemoglobin molecules locked in doubly liganded conformations
- 29 January 1999
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 285 (4) , 1383-1388
- https://doi.org/10.1006/jmbi.1998.2407
Abstract
No abstract availableKeywords
Funding Information
- Ministry of Education, Culture, Sports, Science and Technology
This publication has 25 references indexed in Scilit:
- Conformational Fluctuations in Deoxy Hemoglobin Revealed as a Major Contributor to Anionic Modulation of Function through Studies of the Oxygenation and Oxidation of Hemoglobins A0 and Deer Lodge β2(NA2)His → ArgBiochemistry, 1998
- T State Hemoglobin Binds Oxygen Noncooperatively with Allosteric Effects of Protons, Inositol Hexaphosphate, and ChloridePublished by Elsevier ,1997
- Can a Two-State MWC Allosteric Model Explain Hemoglobin Kinetics?Biochemistry, 1997
- Encapsulation of Proteins in Transparent Porous Silicate Glasses Prepared by the Sol-Gel MethodScience, 1992
- Molecular Code for Cooperativity in HemoglobinScience, 1992
- Proton Nuclear Magnetic Resonance Studies On Hemoglobin: Cooperative Interactions And Partially Ligated IntermediatesAdvances in Protein Chemistry, 1992
- Identification of the intermediate allosteric species in human hemoglobin reveals a molecular code for cooperative switching.Proceedings of the National Academy of Sciences, 1991
- Oxygen Binding in Cyanmet Hybrid and Normal Hemoglobins: Applicability of Sequential and Two-State Concerted ModelsScience, 1974
- Extensions of the Allosteric Model for HaemoglobinNature, 1971
- Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits*Biochemistry, 1966