| Título: | Proteins Are Solitary! Pathways of Protein Folding and Aggregation in Protein Mixtures |
| Autores: | Bianco, Valentino ; Alonso-Navarro, Miren ; Di Silvio, Desire ; Moya, Sergio ; Cortajarena L., Aitziber ; Coluzza, Ivan |
| Tipo de documento: | texto impreso |
| Editorial: | ACS, 2019 |
| Dimensiones: | application/pdf |
| Nota general: | info:eu-repo/semantics/openAccess |
| Idiomas: | |
| Palabras clave: | Estado = En prensa , Materia = Ciencias: Física , Materia = Ciencias: Física: Termodinámica , Materia = Ciencias: Química , Materia = Ciencias Biomédicas: Biología , Tipo = Artículo |
| Resumen: |
We present a computational and experimental study on the folding and aggregation in solutions of multiple protein mixtures at different concentrations. We show how in protein mixtures, each component is capable of maintaining its folded state at desensitises higher then the one at which they would precipitate in single species solutions. We demonstrate the generality of our observation over many different proteins using computer simulations capable of fully characterising the cross-aggregation phase diagram of all the mixtures. Dynamic light Scattering experiments were performed to evaluate the aggregation of two proteins, the bovine serum albumin (BSA) and the consensus tetratricopeptide repeat (CTPR), in solutions of one or both proteins. The experiment confirm our hypothesis and the simulations. These findings elucidate critical aspects on the cross-regulation of expression and aggregation of proteins exerted by the cell and on the evolutionary selection of folding and not-aggregating protein sequences, paving the way for new experimental tests. |
| En línea: | https://eprints.ucm.es/id/eprint/57003/1/Proteins%20Are%20Solitary%21%20Pathways%20of%20Protein%20Folding%20and%20Aggregation%20in%20Protein%20Mixtures%20JUST%20ACCEPTED.pdf |
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