Universality of protein reentrant condensation in solution induced by multivalent metal ions

Publication type:
Journal article
Metadata:
Autoren
  • Fajun Zhang
  • Sophie Weggler
  • Michael J Ziller
  • Luca Ianeselli
  • Benjamin S Heck
  • Andreas Hildebrandt
  • Oliver Kohlbacher
  • Maximilian WA Skoda
  • Robert MJ Jacobs
  • Frank Schreiber
Autoren-URL
https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000284046400018&DestLinkType=FullRecord&DestApp=WOS_CPL
DOI
10.1002/prot.22852
Externe Identifier
  • Clarivate Analytics Document Solution ID: 678CK
  • PubMed Identifier: 20872851
ISSN
0887-3585
Ausgabe der Veröffentlichung
16
Zeitschrift
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Schlüsselwörter
  • charge inversion
  • protein condensation
  • zeta-potential
  • cation binding on protein surface
Paginierung
3450 - 3457
Datum der Veröffentlichung
2010
Status
Published
Titel
Universality of protein reentrant condensation in solution induced by multivalent metal ions
Sub types
  • Article
Ausgabe der Zeitschrift
78

Data source: Web of Science (Lite)

Other metadata sources:
Abstract
<jats:title>Abstract</jats:title><jats:p>The effective interactions and phase behavior of protein solutions under strong electrostatic coupling conditions are difficult to understand due to the complex charge pattern and irregular geometry of protein surfaces. This distinguishes them from related systems such as DNA or conventional colloids. In this work, we discuss the question of universality of the reentrant condensation (RC) of proteins in solution induced by multivalent counterions, i.e., redissolution on adding further salts after phase separation, as recently discovered (Zhang <jats:italic>et al</jats:italic>., Phys Rev Lett 2008; 101:148101). The discussion is based on a systematic investigation of five different proteins with different charge patterns and five different multivalent counterions. Zeta potential measurements confirm the effective charge inversion of proteins in the reentrant regime via binding of multivalent counterions, which is supported by Monte Carlo simulations. Charge inversion by trivalent cations requires an overall negative net charge of the protein. Statistical analysis of a representative set of protein sequences reveals that, in theory, this effect could be possible for about half of all proteins. Our results can be exploited for the control of the phase behavior of proteins, in particular facilitating protein crystallization. Proteins 2010. © 2010 Wiley‐Liss, Inc.</jats:p>
Autoren
  • Fajun Zhang
  • Sophie Weggler
  • Michael J Ziller
  • Luca Ianeselli
  • Benjamin S Heck
  • Andreas Hildebrandt
  • Oliver Kohlbacher
  • Maximilian WA Skoda
  • Robert MJ Jacobs
  • Frank Schreiber
DOI
10.1002/prot.22852
eISSN
1097-0134
ISSN
0887-3585
Ausgabe der Veröffentlichung
16
Zeitschrift
Proteins: Structure, Function, and Bioinformatics
Sprache
en
Online publication date
2010
Paginierung
3450 - 3457
Datum der Veröffentlichung
2010
Status
Published
Herausgeber
Wiley
Herausgeber URL
http://dx.doi.org/10.1002/prot.22852
Datum der Datenerfassung
2023
Titel
Universality of protein reentrant condensation in solution induced by multivalent metal ions
Ausgabe der Zeitschrift
78

Data source: Crossref

Abstract
The effective interactions and phase behavior of protein solutions under strong electrostatic coupling conditions are difficult to understand due to the complex charge pattern and irregular geometry of protein surfaces. This distinguishes them from related systems such as DNA or conventional colloids. In this work, we discuss the question of universality of the reentrant condensation (RC) of proteins in solution induced by multivalent counterions, i.e., redissolution on adding further salts after phase separation, as recently discovered (Zhang et al., Phys Rev Lett 2008; 101:148101). The discussion is based on a systematic investigation of five different proteins with different charge patterns and five different multivalent counterions. Zeta potential measurements confirm the effective charge inversion of proteins in the reentrant regime via binding of multivalent counterions, which is supported by Monte Carlo simulations. Charge inversion by trivalent cations requires an overall negative net charge of the protein. Statistical analysis of a representative set of protein sequences reveals that, in theory, this effect could be possible for about half of all proteins. Our results can be exploited for the control of the phase behavior of proteins, in particular facilitating protein crystallization.
Addresses
  • Institut für Angewandte Physik, Eberhard Karls Universität Tübingen, Auf der Morgenstelle 10, Tübingen 72076, Germany. Fajun.zhang@uni-tuebingen.de
Autoren
  • Fajun Zhang
  • Sophie Weggler
  • Michael J Ziller
  • Luca Ianeselli
  • Benjamin S Heck
  • Andreas Hildebrandt
  • Oliver Kohlbacher
  • Maximilian WA Skoda
  • Robert MJ Jacobs
  • Frank Schreiber
DOI
10.1002/prot.22852
eISSN
1097-0134
Externe Identifier
  • PubMed Identifier: 20872851
Open access
false
ISSN
0887-3585
Ausgabe der Veröffentlichung
16
Zeitschrift
Proteins
Schlüsselwörter
  • Animals
  • Cattle
  • Humans
  • Ions
  • Yttrium
  • Metals
  • Proteins
  • Serum Albumin, Bovine
  • Solutions
  • Monte Carlo Method
  • Hydrogen-Ion Concentration
  • Phase Transition
  • Computer Simulation
  • Static Electricity
Sprache
eng
Medium
Print-Electronic
Online publication date
2010
Paginierung
3450 - 3457
Datum der Veröffentlichung
2010
Status
Published
Datum der Datenerfassung
2010
Titel
Universality of protein reentrant condensation in solution induced by multivalent metal ions.
Sub types
  • Journal Article
Ausgabe der Zeitschrift
78

Data source: Europe PubMed Central

Abstract
The effective interactions and phase behavior of protein solutions under strong electrostatic coupling conditions are difficult to understand due to the complex charge pattern and irregular geometry of protein surfaces. This distinguishes them from related systems such as DNA or conventional colloids. In this work, we discuss the question of universality of the reentrant condensation (RC) of proteins in solution induced by multivalent counterions, i.e., redissolution on adding further salts after phase separation, as recently discovered (Zhang et al., Phys Rev Lett 2008; 101:148101). The discussion is based on a systematic investigation of five different proteins with different charge patterns and five different multivalent counterions. Zeta potential measurements confirm the effective charge inversion of proteins in the reentrant regime via binding of multivalent counterions, which is supported by Monte Carlo simulations. Charge inversion by trivalent cations requires an overall negative net charge of the protein. Statistical analysis of a representative set of protein sequences reveals that, in theory, this effect could be possible for about half of all proteins. Our results can be exploited for the control of the phase behavior of proteins, in particular facilitating protein crystallization.
Date of acceptance
2010
Autoren
  • Fajun Zhang
  • Sophie Weggler
  • Michael J Ziller
  • Luca Ianeselli
  • Benjamin S Heck
  • Andreas Hildebrandt
  • Oliver Kohlbacher
  • Maximilian WA Skoda
  • Robert MJ Jacobs
  • Frank Schreiber
Autoren-URL
https://www.ncbi.nlm.nih.gov/pubmed/20872851
DOI
10.1002/prot.22852
eISSN
1097-0134
Ausgabe der Veröffentlichung
16
Zeitschrift
Proteins
Schlüsselwörter
  • Animals
  • Cattle
  • Computer Simulation
  • Humans
  • Hydrogen-Ion Concentration
  • Ions
  • Metals
  • Monte Carlo Method
  • Phase Transition
  • Proteins
  • Serum Albumin, Bovine
  • Solutions
  • Static Electricity
  • Yttrium
Sprache
eng
Country
United States
Paginierung
3450 - 3457
Datum der Veröffentlichung
2010
Status
Published
Datum, an dem der Datensatz öffentlich gemacht wurde
2011
Titel
Universality of protein reentrant condensation in solution induced by multivalent metal ions.
Sub types
  • Journal Article
Ausgabe der Zeitschrift
78

Data source: PubMed

Autoren
  • Fajun Zhang
  • Sophie Weggler
  • Michael J Ziller
  • Luca Ianeselli
  • Benjamin S Heck
  • Andreas Hildebrandt
  • Oliver Kohlbacher
  • Maximilian WA Skoda
  • Robert MJ Jacobs
  • Frank Schreiber
Zeitschrift
Proteins: Structure, Function, and Bioinformatics
Artikelnummer
16
Paginierung
3450 - 3457
Datum der Veröffentlichung
2010
Herausgeber
Wiley Online Library
Datum der Datenerfassung
2020
Titel
Universality of protein reentrant condensation in solution induced by multivalent metal ions
Sub types
  • article
Ausgabe der Zeitschrift
78

Data source: Manual

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