Fluorescence studies of internal rotation in apohemoglobin alpha-chains.
The molecular dynamics of the apo alpha-chain of human hemoglobin have been examined using three different fluorescent probes, as well as by circular dichroism. All of these criteria are consistent with a significant loss of organized structure and molecular rigidity for the apo derivative. The apo alpha-chain thus contrasts with the apo beta-chain, which retains considerable rigidity and organized structure.
D001059:Apoproteins; D055598:Chemical Phenomena; D002621:Chemistry; D002942:Circular Dichroism; D003545:Cysteine / Q000032:analysis; D004735:Energy Transfer; D006454:Hemoglobins; D006801:Humans; D010446:Peptide Fragments; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D014364:Tryptophan / Q000032:analysis
D001059:Apoproteins; D006454:Hemoglobins; D010446:Peptide Fragments; C023478:apohemoglobin; D014364:Tryptophan; D003545:Cysteine