Influence of Salts on the Phase Behavior of Aqueous-Protein Solutions

2014 ◽  
Vol 86 (9) ◽  
pp. 1505-1505
Author(s):  
C. Brandenbusch ◽  
C. Kress ◽  
G. Sadowski
Keyword(s):  
Phase Behavior ◽  
Protein Solutions

Phase behavior of lysozyme solutions in the liquid–liquid phase coexistence region at high hydrostatic pressures

2016 ◽  
Vol 18 (21) ◽  
pp. 14252-14256 ◽  
Author(s):  
Julian Schulze ◽  
Johannes Möller ◽  
Jonathan Weine ◽  
Karin Julius ◽  
Nico König ◽  
...  
Keyword(s):  
Phase Separation ◽  
Liquid Phase ◽  
Phase Behavior ◽  
High Pressures ◽  
Phase Coexistence ◽  
Protein Solutions ◽  
Separation Region ◽  
Coexistence Region ◽  
High Hydrostatic Pressures ◽  
Liquid Liquid Phase Separation

Dense protein solutions exhibit a reentrant liquid–liquid phase separation region at high pressures.

Strong Isotope Effects on Effective Interactions and Phase Behavior in Protein Solutions in the Presence of Multivalent Ions

2017 ◽  
Vol 121 (7) ◽  
pp. 1731-1739 ◽  
Author(s):  
Michal K. Braun ◽  
Marcell Wolf ◽  
Olga Matsarskaia ◽  
Stefano Da Vela ◽  
Felix Roosen-Runge ◽  
...  
Keyword(s):  
Phase Behavior ◽  
Isotope Effects ◽  
Protein Solutions ◽  
Effective Interactions ◽  
Multivalent Ions

Reentrant Phase Behavior in Protein Solutions Induced by Multivalent Salts: Strong Effect of Anions Cl– Versus NO3–

2018 ◽  
Vol 122 (50) ◽  
pp. 11978-11985 ◽  
Author(s):  
Michal K. Braun ◽  
Andrea Sauter ◽  
Olga Matsarskaia ◽  
Marcell Wolf ◽  
Felix Roosen-Runge ◽  
...  
Keyword(s):  
Phase Behavior ◽  
Protein Solutions

Unification of lower and upper critical solution temperature phase behavior of globular protein solutions in the presence of multivalent cations

Soft Matter ◽  
2020 ◽  
Vol 16 (8) ◽  
pp. 2128-2134 ◽  
Author(s):  
Nafisa Begam ◽  
Olga Matsarskaia ◽  
Michael Sztucki ◽  
Fajun Zhang ◽  
Frank Schreiber
Keyword(s):  
Phase Behavior ◽  
Globular Protein ◽  
Solution Temperature ◽  
Protein Solutions ◽  
Temperature Phase ◽  
Critical Solution Temperature ◽  
Upper Critical Solution Temperature

Here we report that a unified LCST and UCST phase behavior in protein solutions can be achieved by tuning the concentration of multivalent salts.

scholarly journals Role of Entropy in Determining the Phase Behavior of Protein Solutions Induced by Multivalent Ions

Soft Matter ◽  
2021 ◽  
Author(s):  
Anil Kumar Sahoo ◽  
Frank Schreiber ◽  
Roland Netz ◽  
Prabal Kumar Maiti
Keyword(s):  
Aqueous Solutions ◽  
Phase Behavior ◽  
Lower Critical Solution Temperature ◽  
Solution Phase ◽  
Solution Temperature ◽  
Protein Solutions ◽  
Critical Solution Temperature ◽  
Multivalent Ions

Recent experiments have reported lower critical solution temperature (LCST) phase behavior of aqueous solutions of proteins induced by multivalent ions, where the solution phase separates upon heating. This phenomenon is...

Phase Behavior of Poly(sulfobetaine methacrylate)-Grafted Silica Nanoparticles and Their Stability in Protein Solutions

Langmuir ◽  
2011 ◽  
Vol 27 (24) ◽  
pp. 15282-15291 ◽  
Author(s):  
Zhixin Dong ◽  
Jun Mao ◽  
Muquan Yang ◽  
Dapeng Wang ◽  
Shuqin Bo ◽  
...  
Keyword(s):  
Phase Behavior ◽  
Silica Nanoparticles ◽  
Protein Solutions

scholarly journals Kinetics of liquid–liquid phase separation in protein solutions exhibiting LCST phase behavior studied by time-resolved USAXS and VSANS

Soft Matter ◽  
2016 ◽  
Vol 12 (46) ◽  
pp. 9334-9341 ◽  
Author(s):  
Stefano Da Vela ◽  
Michal K. Braun ◽  
Andreas Dörr ◽  
Alessandro Greco ◽  
Johannes Möller ◽  
...  
Keyword(s):  
Phase Separation ◽  
Liquid Phase ◽  
Phase Behavior ◽  
Liquid Phase Separation ◽  
Protein Solutions ◽  
Time Resolved ◽  
Kinetics Of ◽  
Liquid Liquid Phase Separation

Competing Salt Effects on Phase Behavior of Protein Solutions: Tailoring of Protein Interaction by the Binding of Multivalent Ions and Charge Screening

2014 ◽  
Vol 118 (38) ◽  
pp. 11365-11374 ◽  
Author(s):  
Elena Jordan ◽  
Felix Roosen-Runge ◽  
Sara Leibfarth ◽  
Fajun Zhang ◽  
Michael Sztucki ◽  
...  
Keyword(s):  
Phase Behavior ◽  
Protein Interaction ◽  
Protein Solutions ◽  
Salt Effects ◽  
Charge Screening ◽  
Multivalent Ions

Characterization of frozen hydrated biological specimens by low-loss EELS

1992 ◽  
Vol 50 (2) ◽  
pp. 1572-1573
Author(s):  
Songquan Sun ◽  
Richard D. Leapman
Keyword(s):  
Water Content ◽  
Direct Method ◽  
Internal Standard ◽  
Dry Weight ◽  
Dark Field ◽  
Protein Solutions ◽  
Subcellular Compartment ◽  
Differential Shrinkage ◽  
Electron Energy Loss

Analyses of ultrathin cryosections are generally performed after freeze-drying because the presence of water renders the specimens highly susceptible to radiation damage. The water content of a subcellular compartment is an important quantity that must be known, for example, to convert the dry weight concentrations of ions to the physiologically more relevant molar concentrations. Water content can be determined indirectly from dark-field mass measurements provided that there is no differential shrinkage between compartments and that there exists a suitable internal standard. The potential advantage of a more direct method for measuring water has led us to explore the use of electron energy loss spectroscopy (EELS) for characterizing biological specimens in their frozen hydrated state.We have obtained preliminary EELS measurements from pure amorphous ice and from cryosectioned frozen protein solutions. The specimens were cryotransfered into a VG-HB501 field-emission STEM equipped with a 666 Gatan parallel-detection spectrometer and analyzed at approximately −160 C.

Phase behavior of cationic and anionic surfactants at low concentrations

1992 ◽  
Vol 50 (1) ◽  
pp. 694-695
Author(s):  
E. Naranjo
Keyword(s):  
Phase Behavior ◽  
Structural Characterization ◽  
Dynamic Systems ◽  
Anionic Surfactants ◽  
Intermolecular Forces ◽  
Stable Form ◽  
Surfactant Mixtures ◽  
Low Concentrations ◽  
Cationic And Anionic Surfactants ◽  
General Method

Equilibrium vesicles, those which are the stable form of aggregation and form spontaneously on mixing surfactant with water, have never been demonstrated in single component bilayers and only rarely in lipid or surfactant mixtures. Designing a simple and general method for producing spontaneous and stable vesicles depends on a better understanding of the thermodynamics of aggregation, the interplay of intermolecular forces in surfactants, and an efficient way of doing structural characterization in dynamic systems.

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