Open AccessConformational Studies of Various Hemoglobins by Natural-Abundance 13 C NMR Spectroscopy
Author(s) -
Richard B. Moon,
John H. Richards
Publication year - 1972
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.69.8.2193
Subject(s) - tetramer , protein quaternary structure , chemistry , nuclear magnetic resonance spectroscopy , abundance (ecology) , beta (programming language) , spectroscopy , stereochemistry , crystallography , biochemistry , enzyme , biology , protein subunit , physics , quantum mechanics , fishery , gene , computer science , programming language
Studies of variously liganded hemoglobins (both from human and rabbit) by natural-abundance13 C NMR spectroscopy have revealed apparent conformational differences that have been interpreted on the basis of two quaternary structures for the α2 β2 tetramer, and variable tertiary structures for the individual α and β subunits. In solution, rabbit hemoglobins appear to have somewhat more flexibility than human hemoglobins.