Study of chaperone-like activity of human haptoglobin: conformational changes under heat shock conditions and localization of interaction sites
| Autor: | Rüdiger Ettrich, Katerina Hofbauerova, Vladimír Kopecký, Wolfgang Brandt, Zdenek Pavlícek, Vladimír Baumruk |
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| Rok vydání: | 2002 |
| Předmět: |
Models
Molecular Circular dichroism Protein Denaturation Hot Temperature Clinical Biochemistry Molecular Sequence Data Biochemistry Protein Structure Secondary Hemoglobins Protein structure Tetramer Heat shock protein polycyclic compounds Humans Amino Acid Sequence skin and connective tissue diseases Molecular Biology Protein secondary structure Peptide sequence Heat-Shock Proteins Binding Sites biology Haptoglobins Sequence Homology Amino Acid Chemistry Spectrum Analysis Haptoglobin Titrimetry food and beverages Catalase Chaperone (protein) biology.protein Biophysics Solvents Thermodynamics Sequence Alignment Molecular Chaperones |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 1431-6730 |
| Popis: | With respect to the mechanism of chaperone-like activity, we examined the behavior of haptoglobin under heat shock conditions. Secondary structure changes during heat treatment were followed by circular dichroism, Raman and infrared spectroscopy. A model of the haptoglobin tetramer, based on its sequence homology with serine proteases and the CCP modules, has been proposed. Sequence regions responsible for the chaperone-like activity were not fully identical with the region that takes part in formation of the hemoglobin-haptoglobin complex. We can postulate the presence of at least two different chaperone-binding sites on each haptoglobin heavy chain. |
| Databáze: | OpenAIRE |
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