Data concerning secondary structure and alpha-glucans-binding capacity of the LaCBM26
| Autor: | Karen Manoutcharian, Zaira Sánchez-Cuapio, Sergio Sánchez, Silvia Armenta, Amelia Farrés, Romina Rodríguez-Sanoja, Alejandra Hernández-Santoyo |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
chemistry.chemical_classification Gel electrophoresis Circular dichroism Multidisciplinary biology Hydrogen bond Stereochemistry Substrate (chemistry) Isothermal titration calorimetry Starch biology.organism_classification lcsh:Computer applications to medicine. Medical informatics 03 medical and health sciences 030104 developmental biology Enzyme chemistry Lactobacillus Biochemistry Genetics and Molecular Biology α-Glucans recognition lcsh:R858-859.7 lcsh:Science (General) Protein secondary structure Carbohydrate-binding module lcsh:Q1-390 |
| Zdroj: | Data in Brief Data in Brief, Vol 21, Iss, Pp 1944-1949 (2018) |
| ISSN: | 2352-3409 |
| Popis: | Carbohydrate-binding modules (CBMs) are auxiliary domains into glycoside-hydrolases that allow the interaction between the insoluble substrate and the solubilized enzyme, through hydrophobic, CH-π interactions and hydrogen bonds. Here, we present the data article related to the interaction of one LaCBM26 and some mutated proteins with soluble α-glucans determined by enzyme-linked carbohydrate-binding assay, isothermal titration calorimetry (ITC), and affinity gel electrophoresis (AGE). The data of the behavior of proteins in presence and absence of substrate analyzed by circular dichroism CD and thermofluor are also presented. These results are complementary to the research article “The role of conserved non-aromatic residues in the Lactobacillus amylovorus α-amylase CBM26-starch interaction” (Armenta et al., 2019). Keywords: Carbohydrate-binding module, Starch, α-Glucans recognition |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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