Fluorescence studies of internal rotation in apohemoglobin alpha-chains
| Autor: | José Manuel Otón, Enrico Bucci, Robert F. Steiner, Clara Fronticelli, Asuncion Martinez, Dionigio Franchi |
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| Rok vydání: | 1984 |
| Předmět: |
Circular dichroism
Chemical Phenomena Chemistry Protein Conformation Circular Dichroism Internal rotation Biophysics Tryptophan Biochemistry Fluorescence Peptide Fragments Molecular dynamics Crystallography Hemoglobins Rigidity (electromagnetism) Spectrometry Fluorescence Energy Transfer Apohemoglobin Humans lipids (amino acids peptides and proteins) Hemoglobin Cysteine Apoproteins Molecular Biology |
| Zdroj: | Archives of biochemistry and biophysics. 228(2) |
| ISSN: | 0003-9861 |
| Popis: | The molecular dynamics of the apo α-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 α-chain thus contrasts with the apo β-chain, which retains considerable rigidity and organized structure. |
| Databáze: | OpenAIRE |
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