Relative Stability of Human Centrins and Its Relationship to Calcium Binding
| Autor: | Lizbeth Irizarry, Belinda Pastrana-Rios, Verónica Meza, Adalberto Díaz Casas, Mara Colón, Myrna Reyes, Melissa Campbell, Ana María Gómez, Aslin Rodríguez Nassif, José Robles, Ana María Ortiz, Jessica De Orbeta, Ruth Almodovar, Daniel Narváez |
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| Rok vydání: | 2013 |
| Předmět: |
Protein Denaturation
Circular dichroism Protein Conformation Molecular Sequence Data Cell Cycle Proteins Biochemistry Article 03 medical and health sciences 0302 clinical medicine Protein structure Calcium-binding protein Spectroscopy Fourier Transform Infrared Humans Denaturation (biochemistry) Amino Acid Sequence Binding site Cell Cycle Protein 030304 developmental biology 0303 health sciences Binding Sites Calorimetry Differential Scanning Chemistry Circular Dichroism Spectrum Analysis Calcium-Binding Proteins Biological target Calcium Two-dimensional nuclear magnetic resonance spectroscopy 030217 neurology & neurosurgery |
| Zdroj: | Biochemistry |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi301417z |
| Popis: | Centrins are calcium binding proteins that belong to the EF-hand superfamily with diverse biological functions. Herein we present the first systematic study that establishes the relative stability of related centrins via complementary biophysical techniques. Our results define the stepwise molecular behavior of human centrins by two-dimensional infrared (2D IR) correlation spectroscopy, the change in heat capacity and enthalpy of denaturation by differential scanning calorimetry, and the relative stability of the helical regions of centrins by circular dichroism. More importantly, 2D IR correlation spectroscopy provides unique information about the similarities and differences in dynamics between these related proteins. The thermally induced molecular behavior of human centrins can be used to predict biological target interactions that have a relative dependence on calcium affinity. This information is essential for understanding why certain isoforms may be used to rescue a phenotype and therefore also for explaining the different functions these proteins may have in vivo. Furthermore, this comparative approach can be applied to the study of recombinant therapeutic protein candidates for the treatment of disease states. |
| Databáze: | OpenAIRE |
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