Conformational Studies of Various Hemoglobins by Natural-Abundance 13C NMR Spectroscopy
AUTOR(ES)
Moon, R. B.
RESUMO
Studies of variously liganded hemoglobins (both from human and rabbit) by natural-abundance 13C NMR spectroscopy have revealed apparent conformational differences that have been interpreted on the basis of two quaternary structures for the α2β2 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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=426898Documentos Relacionados
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