Denaturation of proteins: electrostatic effects <i>vs.</i> hydration

Ballauff, Matthias

doi:10.1039/d2ra01167k

Cited by 3 publications

(3 citation statements)

References 60 publications

(197 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This choice is well-borne out of various experimental studies on complex formation , and of protein denaturation in solution (cf. the discussion of this point in ref ). Then for a given T 0 = 265 K, a secure fit of all data displayed in Figure a can be easily reached.…”

Section: Resultsmentioning

confidence: 97%

“…Hence, the temperature T 0 is directly related to hydrations effects. We recently showed that this concept is also applicable to the unfolding of proteins …”

Section: Introductionmentioning

confidence: 99%

“…We recently showed that this concept is also applicable to the unfolding of proteins. 62 The model has first been applied to the binding of heparin to lysozyme 61 and to the binding of two synthetic polyelectrolytes to bovine serum albumin. 63 The entire derivation of the model shows that temperature T and salt concentration c s are the two decisive variables that influence the free energy of binding.…”

Section: ■ Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Interaction of Heparin with Proteins: Hydration Effects

2022

Self Cite

View full text Add to dashboard Cite

We present a thermodynamic investigation of the interaction of heparin with lysozyme in the presence of potassium glutamate (KGlu). The binding constant K b is measured by isothermal titration calorimetry (ITC) in a temperature range from 288 to 310 K for concentrations of KGlu between 25 and 175 mM. The free energy of binding ΔG b derived from K b is strongly decreasing with increasing concentration of KGlu, whereas the dependence of ΔG b on temperature T is found to be small. The decrease of ΔG b can be explained in terms of counterion release: Binding of lysozyme to the strong polyelectrolyte heparin liberates approximately three of the condensed counterions of heparin, thus increasing the entropy of the system. The dependence of ΔG b on T, on the other hand, is traced back to a change of hydration of the protein and the polyelectrolyte upon complex formation. This dependence is quantitatively described by the parameter Δw that depends on T and vanishes at a characteristic temperature T 0. A comparison of the complex formation in the presence of KGlu with the one in the presence of NaCl demonstrates that the parameters related to hydration are changed considerably. The characteristic temperature T 0 in the presence of KGlu solutions is considerably smaller than that in the presence of NaCl solutions. The change of specific heat Δc p is found to become more negative with increasing salt concentration: This finding agrees with the model-free analysis by the generalized van’t Hoff equation. The entire analysis reveals a small but important change of the free energy of binding by hydration. It shows that these ion-specific Hofmeister effects can be modeled quantitatively in terms of a characteristic temperature T 0 and a parameter describing the dependence of Δc p on salt concentration.

show abstract

Section: Resultsmentioning

confidence: 97%

“…Hence, the temperature T 0 is directly related to hydrations effects. We recently showed that this concept is also applicable to the unfolding of proteins …”

Section: Introductionmentioning

confidence: 99%

Section: ■ Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Interaction of Heparin with Proteins: Hydration Effects

2022

Self Cite

View full text Add to dashboard Cite

show abstract

Synthesis of Asymmetric Ionic Hybrid Detergents enables Micelles with Scalable Properties including Cell Compatibility

Wycisk,

Behnke,

Nielinger

et al. 2024

Chemistry A European J

View full text Add to dashboard Cite

Ionic detergents enable applications and cause harm in biospheres due to cell toxicity. The utility of covalent combinations between ionic and non‐ionic detergent headgroups in modulating cell toxicity remains speculative due to the yet rarely explored synthesis. We close this gap and establish the modular synthesis of ionic/non‐ionic hybrid detergents. We restructure a combinatorial methallyl dichloride one‐pot coupling into a two‐step coupling, which reduces by‐products, improves product yields, and enables the gram‐scale preparation of asymmetric, cationic/non‐ionic and anionic/non‐ionic hybrid detergents. Our modular synthesis delivers new modalities for the design of ionic detergents, including an unprecedented scaling of properties that determine applications, such as charge, critical micelle concentration (cmc), solubilizing properties, hard water tolerance, and cell compatibility. We uncover that shielding the charge in ionic headgroups can switch the detergent species that is toxic to cells from monomers to mixtures of monomers and micellar assemblies. Establishing the chemistry of ionic/non‐ionic hybrid detergents provides a missing evolutionary link in the structural comparison of ionic and non‐ionic detergents, enables an easy synthesis access to yet unexplored chemical spaces of asymmetric hybrid materials, and delivers new modalities for designing the toxicity of supramolecular nanomaterials.

show abstract

Correlation between Water Characteristics and Gel Strength in the Gel Formation of Golden Pompano Surimi Induced by Dense Phase Carbon Dioxide

Duan

Qiu

Htwe

et al. 2023

Foods

View full text Add to dashboard Cite

The relationship between the gel quality of golden pompano surimi treated with dense phase carbon dioxide (DPCD) and changes in water characteristics was evaluated. Low-field nuclear magnetic resonance (LF-NMR) and nuclear magnetic resonance imaging were used to monitor changes in the water status of surimi gel under different treatment conditions. Whiteness, water-holding capacity and gel strength were used as the quality indicators of the surimi gel. The results showed that DPCD treatment could significantly increase the whiteness of surimi and the strength of the gel, while the water-holding capacity decreased significantly. LF-NMR analysis showed that, as the DPCD treatment intensity increased, the relaxation component T22 shifted to the right, T23 shifted to the left, the proportion of A22 decreased significantly (p < 0.05) and the proportion of A23 increased significantly (p < 0.05). A correlation analysis of water characteristics and gel strength showed that the water-holding capacity of surimi induced by DPCD was strongly positively correlated with gel strength, while A22 and T23 were strongly negatively correlated with gel strength. This study provides helpful insights into the quality control of DPCD in surimi processing and also provides an approach for the quality evaluation and detection of surimi products.

show abstract

Denaturation of proteins: electrostatic effects vs. hydration

Abstract: A phenomenological approach to the unfolding transition of proteins is given. The model treats quantitatively the effect of electrostatics as well as of hydration (Hofmeister effects).

Cited by 3 publications

References 60 publications

Interaction of Heparin with Proteins: Hydration Effects

Interaction of Heparin with Proteins: Hydration Effects

Synthesis of Asymmetric Ionic Hybrid Detergents enables Micelles with Scalable Properties including Cell Compatibility

Correlation between Water Characteristics and Gel Strength in the Gel Formation of Golden Pompano Surimi Induced by Dense Phase Carbon Dioxide

Contact Info

Product

Resources

About