Print Email Facebook Twitter Dynamic structure of human serum transferrin from transient electric birefringence experiments Title Dynamic structure of human serum transferrin from transient electric birefringence experiments Author TNO Voeding van Haeringen, B. de Lange, F. van Stokkum, I.H.M. Srai, S.K.S. Evans, R.W. van Grondelle, R. Bloemendal, M. Publication year 1995 Abstract In order to investigate the secondary, tertiary, and dynamic structure of the iron-free (apo) and iron-saturated (holo) forms of human serum transferrin and its amino (N)-terminal lobe at the physiologically relevant pHs 7.4 and 5.0, we have combined ultraviolet circular dichroism (CD) spectroscopy with transient-electric birefringence (TEB) measurements. No significant changes are found in the protein's secondary structure under the different conditions studied. The tertiary structure as monitored by near-UV CD is affected by iron binding, but does not change upon decrease in pH. In contrast, TEB results indicate dramatic changes in the dynamic structure of transferrin both upon binding of iron and decrease of pH. In apotransferrin freedom of movement is found for the lobes with respect to each other, and for the domains within the lobes. The interlobal flexibility is considerably enhanced at the lower pH. Holotransferrin is found to behave as a rigid molecule. Subject Kerr effectApoproteinsBirefringenceCircular DichroismEndocytosisHumanHydrogen-Ion ConcentrationIronMotionProtein Structure, SecondaryProtein Structure, TertiaryTransferrin To reference this document use: http://resolver.tudelft.nl/uuid:0f516cd4-937e-41e0-8031-0e11584603e8 DOI https://doi.org/10.1002/prot.340230212 TNO identifier 233065 ISSN 0887-3585 Source Proteins: Structure, Function and Genetics, 23 (23), 233-240 Document type article Files To receive the publication files, please send an e-mail request to TNO Library.