RT Journal Article
T1 Proteins Are Solitary! Pathways of Protein Folding and Aggregation in Protein Mixtures
A1 Bianco, Valentino
A1 Alonso-Navarro, Miren
A1 Di Silvio, Desire
A1 Moya, Sergio
A1 Cortajarena L., Aitziber
A1 Coluzza, Ivan
AB 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 phasediagram of all the mixtures. Dynamic light Scattering experiments were performed to evaluate the aggregation of two proteins, the bovine serum albumin (BSA) and theconsensus 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.
PB ACS
SN 1948-7185
YR 2019
FD 2019
LK https://hdl.handle.net/20.500.14352/13559
UL https://hdl.handle.net/20.500.14352/13559
LA eng
NO Unión Europea. H2020
NO Ministerio de Economía y Competitividad (MINECO)
NO Austrian Science Fund (FWF)
NO Unidad de Excelencia "María de Maeztu"
NO Basque Government
DS Docta Complutense
RD 27 abr 2025