Conformational stability of adrenodoxin mutant proteins
| Autor: | O. Ristau, H. Uhlmann, Rita Bernhardt, Wolfgang Pfeil, V. Beckert, Tatiana V. Burova |
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| Rok vydání: | 1996 |
| Předmět: |
Models
Molecular Isothermal microcalorimetry Protein Denaturation Protein Conformation Mutant Thermolysin Calorimetry Biochemistry Structure-Activity Relationship Protein structure Drug Stability Adrenodoxin Denaturation (biochemistry) Molecular Biology Ferredoxin Molecular Structure Chemistry Wild type Crystallography Spectrophotometry Mutagenesis Site-Directed Thermodynamics Oxidation-Reduction Gene Deletion Research Article |
| Zdroj: | Protein Science. 5:1890-1897 |
| ISSN: | 1469-896X 0961-8368 |
| DOI: | 10.1002/pro.5560050915 |
| Popis: | Adrenodoxin and the mutants at the positions T54, H56, D76, Y82, and C95, as well as the deletion mutants 4-114 and 4-108, were studied by high-sensitivity scanning microcalorimetry, limited proteolysis, and absorption spectroscopy. The mutants show thermal transition temperatures ranging from 46 to 56 degrees C, enthalpy changes from 250 to 370 kJ/mol, and heat capacity change delta Cp = 7.28 +/- 0.67 kJ/mol/K, except H56R. The amino acid replacement H56R produces substantial local changes in the region around positions 56 and Y82, as indicated by reduced heat capacity change (delta Cp = 4.29 +/- 0.37 kJ/mol/K) and enhanced fluorescence. Deletion mutant 4-108 is apparently more stable than the wild type, as judged by higher specific denaturation enthalpy and resistance toward proteolytic degradation. No simple correlation between conformational stability and functional properties could be found. |
| Databáze: | OpenAIRE |
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