Moon R B, Richards J H
Proc Natl Acad Sci U S A. 1972 Aug;69(8):2193-7. doi: 10.1073/pnas.69.8.2193.
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.
通过天然丰度的(13)C核磁共振光谱对各种配体结合的血红蛋白(来自人类和兔子)进行的研究揭示了明显的构象差异,这些差异已根据α(2)β(2)四聚体的两种四级结构以及单个α和β亚基的可变三级结构进行了解释。在溶液中,兔子血红蛋白似乎比人类血红蛋白具有更大的灵活性。