Testing mixing rules for structural and dynamical quantities in multi-component crowded protein solutions.


Journal

APL bioengineering
ISSN: 2473-2877
Titre abrégé: APL Bioeng
Pays: United States
ID NLM: 101726398

Informations de publication

Date de publication:
Jun 2024
Historique:
received: 20 02 2024
accepted: 14 05 2024
medline: 3 6 2024
pubmed: 3 6 2024
entrez: 3 6 2024
Statut: epublish

Résumé

Crowding effects significantly influence the phase behavior and the structural and dynamic properties of the concentrated protein mixtures present in the cytoplasm of cells or in the blood serum. This poses enormous difficulties for our theoretical understanding and our ability to predict the behavior of these systems. While the use of course grained colloid-inspired models allows us to reproduce the key physical solution properties of concentrated monodisperse solutions of individual proteins, we lack corresponding theories for complex polydisperse mixtures. Here, we test the applicability of simple mixing rules in order to predict solution properties of protein mixtures. We use binary mixtures of the well-characterized bovine eye lens proteins

Identifiants

pubmed: 38827499
doi: 10.1063/5.0204201
pii: 5.0204201
pmc: PMC11143939
doi:

Types de publication

Journal Article

Langues

eng

Pagination

026116

Informations de copyright

© 2024 Author(s).

Déclaration de conflit d'intérêts

The authors have no conflicts to disclose.

Auteurs

Alessandro Gulotta (A)

Division for Physical Chemistry, Lund University, Naturvetarvägen 14, 22100 Lund, Sweden.

Saskia Bucciarelli (S)

Division for Physical Chemistry, Lund University, Naturvetarvägen 14, 22100 Lund, Sweden.

Olaf Holderer (O)

Jülich Centre for Neutron Science (JCNS) at Heinz Maier-Leibnitz Zentrum (MLZ), Forschungszentrum Jülich GmbH, Garching, Germany.

Classifications MeSH