Nonlinear Impact of Electrolyte Solutions on Protein Dynamics

Abstract: Halophilic organisms have adapted to multi‐molar salt concentrations, their cytoplasmic proteins functioning despite stronger attraction between hydrophobic groups. These proteins, of interest in biotechnology because of decreasing fresh‐water resources, have excess acidic amino acids. It has been suggested that conformational fluctuations – critical for protein function – decrease in the presence of a stronger hydrophobic effect, and that an acidic proteome would counteract this decrease. However, our understanding of the salt‐ and acidic amino acid dependency of enzymatic activity is limited. Here, using solution NMR relaxation and molecular dynamics simulations for in total 14 proteins, we show that salt concentration has a limited and moreover non‐monotonic impact on protein dynamics. The results speak against the conformational‐fluctuations model, instead indicating that maintaining protein dynamics to ensure protein function is not an evolutionary driving force behind the acidic proteome of halophilic proteins.

Angaben zum Objekt

• Standort: Deutsche Nationalbibliothek Frankfurt am Main
• Umfang: Online-Ressource
• Sprache: Englisch

Verweise und Beziehungen

• Erschienen in: Nonlinear Impact of Electrolyte Solutions on Protein Dynamics ; day:16 ; month:05 ; year:2024 ; extent:13 ; ChemBioChem ; (16.05.2024) (gesamt 13)

Beteiligte, Orts- und Zeitangaben

• Urheber: Geraili Daronkola, Hosein ; Söldner, Benedikt ; Singh, Himanshu ; Linser, Rasmus ; Vila Verde, Ana

Weitere Informationen

• DOI: 10.1002/cbic.202400057
• URN: urn:nbn:de:101:1-2405171406102.083149096598
• Rechteinformation: Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
• Letzte Aktualisierung: 14.08.2025, 10:54 MESZ