Residual helicity at the active site of the histidine phosphocarrier, HPr, modulates binding affinity to its natural partners
18 pags., 4 figs., 5 tabs. -- This article belongs to the Special Issue Folding and Design of α-Helical Proteins and Peptides: Theory Meets Nanomaterials, Biotechnology and Health
| Autores: | , , , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2021 |
| País: | España |
| Institución: | Consejo Superior de Investigaciones Científicas (CSIC) |
| Repositorio: | DIGITAL.CSIC. Repositorio Institucional del CSIC |
| OAI Identifier: | oai:digital.csic.es:10261/256259 |
| Acceso en línea: | http://hdl.handle.net/10261/256259 |
| Access Level: | acceso abierto |
| Palabra clave: | Binding Circular dichroism Peptides Isothermal titration calorimetry NMR Fluorescence |
| Sumario: | 18 pags., 4 figs., 5 tabs. -- This article belongs to the Special Issue Folding and Design of α-Helical Proteins and Peptides: Theory Meets Nanomaterials, Biotechnology and Health |
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