Small-angle neutron scattering study of halophilic glyceraldehyde 3-phosphate dehydrogenase (hGAPDH)
| Autor: | Wijaya Altekar, Christine Ebel, Giuseppe Zaccai, Gomathi Krishnan |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
chemistry.chemical_classification
biology Chemistry Axial ratio Salt (chemistry) Concentration effect Neutron scattering Condensed Matter Physics Small-angle neutron scattering Halophile Electronic Optical and Magnetic Materials Crystallography biology.protein Radius of gyration Electrical and Electronic Engineering Glyceraldehyde 3-phosphate dehydrogenase |
| Zdroj: | Physica B: Condensed Matter. 174:306-308 |
| ISSN: | 0921-4526 |
| DOI: | 10.1016/0921-4526(91)90622-l |
| Popis: | hGAPDH has a radius of gyration of 32±0.5 A in high salt concentration, and a shape similar to an oblate ellipsoid of axial ratio 0.5 but with a much larger specific surface. The enzyme dissociates and unfolds in low salt solutions. These results are discussed in terms of the halophilic character of the protein. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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