Proteins are Solitary! Pathways of Protein Folding and Aggregation in Protein Mixtures.
J Phys Chem Lett
; 10(17): 4800-4804, 2019 Sep 05.
Article
em En
| MEDLINE
| ID: mdl-31373499
ABSTRACT
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 densities greater than 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 characterizing the cross-aggregation phase diagram of all the mixtures. Dynamic light scattering experiments were performed to evaluate the aggregation of two proteins, bovine serum albumin (BSA) and consensus tetratricopeptide repeat (CTPR), in solutions of one or both proteins. The experiments confirm our hypothesis and the simulations. These findings elucidate critical aspects of the cross-regulation of expression and aggregation of proteins exerted by the cell and on the evolutionary selection of folding and non-aggregating protein sequences, paving the way for new experimental tests.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Soroalbumina Bovina
/
Agregados Proteicos
Idioma:
En
Ano de publicação:
2019
Tipo de documento:
Article