Universidad Complutense de Madrid
E-Prints Complutense

Proteins Are Solitary! Pathways of Protein Folding and Aggregation in Protein Mixtures



Downloads per month over past year

Bianco, Valentino and Alonso-Navarro, Miren and Di Silvio, Desire and Moya, Sergio and Cortajarena L., Aitziber and Coluzza, Ivan (2019) Proteins Are Solitary! Pathways of Protein Folding and Aggregation in Protein Mixtures. The Journal of Physical Chemistry Letters, 10 (17). pp. 4800-4807. ISSN 1948-7185 (In Press)

[img] PDF
Restringido a Repository staff only hasta 2 August 2020.


Official URL: https://doi.org/10.1021/acs.jpclett.9b01753


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.

Item Type:Article
Uncontrolled Keywords:Light scattering, Mammals, Mixtures
Subjects:Sciences > Physics
Sciences > Physics > Thermodynamics
Sciences > Chemistry
Medical sciences > Biology
ID Code:57003
Deposited On:20 Sep 2019 08:11
Last Modified:24 Sep 2019 11:03

Origin of downloads

Repository Staff Only: item control page