Allosteric sensitivity in hemoglobin at the .alpha.-subunit N-terminus studied by hydrogen exchange
- 1 May 1986
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 25 (10) , 3000-3007
- https://doi.org/10.1021/bi00358a040
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 17 references indexed in Scilit:
- Probing the energetics of proteins through structural perturbation: sites of regulatory energy in human hemoglobin.Proceedings of the National Academy of Sciences, 1982
- Rapid measurement of free amino acids in serum and CSF using high-performance liquid chromatographyLife Sciences, 1981
- Hydrogen exchange from identified regions of the S-protein component of ribonuclease as a function of temperature, pH, and the binding of S-peptideJournal of Molecular Biology, 1981
- The slowest allosterically responsive hydrogens in hemoglobin. Completion of the hydrogen exchange survey.Journal of Biological Chemistry, 1980
- A high energy structure change in hemoglobin studied by difference hydrogen exchange.Journal of Biological Chemistry, 1980
- An experimental procedure for increasing the structural resolution of chemical hydrogen-exchange measurements on proteins: Application to ribonuclease S peptideJournal of Molecular Biology, 1979
- Rapid separation of the α,β,Gγ and Aγ human globin chains by reversed-phase high pressure liquid chromatographyBiochemical and Biophysical Research Communications, 1979
- Haemoglobin: The structural changes related to ligand binding and its allosteric mechanismJournal of Molecular Biology, 1979
- The structure of horse methaemoglobin at 2.0 Å resolutionJournal of Molecular Biology, 1977
- Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits*Biochemistry, 1966