| Literature DB >> 4506089 |
Abstract
Studies of variously liganded hemoglobins (both from human and rabbit) by natural-abundance (13)C NMR spectroscopy have revealed apparent conformational differences that have been interpreted on the basis of two quaternary structures for the alpha(2)beta(2) tetramer, and variable tertiary structures for the individual alpha and beta subunits. In solution, rabbit hemoglobins appear to have somewhat more flexibility than human hemoglobins.Entities:
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Year: 1972 PMID: 4506089 PMCID: PMC426898 DOI: 10.1073/pnas.69.8.2193
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205