scholarly journals Effect of Arginine on Chaperone-Like Activity of HspB6 and Monomeric 14-3-3ζ

2020 ◽  
Vol 21 (6) ◽  
pp. 2039 ◽  
Author(s):  
Valeriya V. Mikhaylova ◽  
Tatiana B. Eronina ◽  
Natalia A. Chebotareva ◽  
Vladimir V. Shubin ◽  
Daria I. Kalacheva ◽  
...  
Keyword(s):  
Conformational Changes ◽  
Glycogen Phosphorylase ◽  
Test System ◽  
Monomeric Form ◽  
Thermal Aggregation ◽  
Scanning Calorimetry ◽  
Glycogen Phosphorylase B ◽  
Protein Chaperones ◽  
Aggregation Activity ◽  
Thermal Stability Of

The effect of protein chaperones HspB6 and the monomeric form of the protein 14-3-3ζ (14-3-3ζm) on a test system based on thermal aggregation of UV-irradiated glycogen phosphorylase b (UV-Phb) at 37 °C and a constant ionic strength (0.15 M) was studied using dynamic light scattering. A significant increase in the anti-aggregation activity of HspB6 and 14-3-3ζm was demonstrated in the presence of 0.1 M arginine (Arg). To compare the effects of these chaperones on UV-Phb aggregation, the values of initial stoichiometry of the chaperone–target protein complex (S0) were used. The analysis of the S0 values shows that in the presence of Arg fewer chaperone subunits are needed to completely prevent aggregation of the UV-Phb subunit. The changes in the structures of HspB6 and 14-3-3ζm induced by binding of Arg were evaluated by the fluorescence spectroscopy and differential scanning calorimetry. It was suggested that Arg caused conformational changes in chaperone molecules, which led to a decrease in the thermal stability of protein chaperones and their destabilization.

Effect of α-crystallin on thermal aggregation of glycogen phosphorylase b from rabbit skeletal muscle

2007 ◽  
Vol 72 (5) ◽  
pp. 518-528 ◽  
Author(s):  
A. V. Meremyanin ◽  
T. B. Eronina ◽  
N. A. Chebotareva ◽  
S. Yu. Kleimenov ◽  
I. K. Yudin ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Glycogen Phosphorylase ◽  
Rabbit Skeletal Muscle ◽  
Thermal Aggregation ◽  
Glycogen Phosphorylase B

scholarly journals Allosteric interactions of glycogen phosphorylase b. A crystallographic study of glucose 6-phosphate and inorganic phosphate binding to di-imidate-cross-linked phosphorylase b

1984 ◽  
Vol 218 (1) ◽  
pp. 45-60 ◽  
Author(s):  
A Lorek ◽  
K S Wilson ◽  
M S P Sansom ◽  
D I Stuart ◽  
E A Stura ◽  
...  
Keyword(s):  
Binding Site ◽  
Conformational Changes ◽  
Inorganic Phosphate ◽  
Glycogen Phosphorylase ◽  
Phosphate Binding ◽  
Binding Studies ◽  
Structural Explanation ◽  
Alpha Helices ◽  
Allosteric Effector ◽  
Glycogen Phosphorylase B

The binding to glycogen phosphorylase b of glucose 6-phosphate and inorganic phosphate (respectively allosteric inhibitor and substrate/activator of the enzyme) were studied in the crystal at 0.3 nm (3A) resolution. Glucose 6-phosphate binds in the alpha-configuration at a site that is close to the AMP allosteric effector site at the subunit-subunit interface and promotes several conformational changes. The phosphate-binding site of the enzyme for glucose 6-phosphate involves contacts to two cationic residues, Arg-309 and Lys-247. This site is also occupied in the inorganic-phosphate-binding studies and is therefore identified as a high-affinity phosphate-binding site. It is distinct from the weaker phosphate-binding site of the enzyme for AMP, which is 0.27 nm (2.7A) away. The glucose moiety of glucose 6-phosphate and the adenosine moiety of AMP do not overlap. The results provide a structural explanation for the kinetic observations that glucose 6-phosphate inhibition of AMP activation of phosphorylase b is partially competitive and highly co-operative. The results suggest that the transmission of allosteric conformational changes involves an increase in affinity at phosphate-binding sites and relative movements of alpha-helices. In order to study glucose 6-phosphate and phosphate binding it was necessary to cross-link the crystals. The use of dimethyl malondi-imidate as a new cross-linking reagent in protein crystallography is discussed.

scholarly journals Anionic surfactant sulfate dodecyl sodium (SDS)-induced thermodynamics and conformational changes of collagen by ultrasensitive microcalorimetry

2021 ◽  
Vol 3 (1) ◽  
Author(s):  
Jie Zhang ◽  
Chunhua Wang ◽  
Fengteng Zhang ◽  
Wei Lin
Keyword(s):  
Thermal Stability ◽  
Conformational Changes ◽  
Triple Helix ◽  
Striking Difference ◽  
Thermal Transition ◽  
Scanning Calorimetry ◽  
Helix Structure ◽  
Stabilizing Effect ◽  
Collagen Molecules ◽  
Thermal Stability Of

Abstract In this communication, sulfate dodecyl sodium (SDS)-induced thermodynamics and conformational changes of collagen were studied. We used ultrasensitive differential scanning calorimetry (US-DSC) to directly monitor the thermal transition of collagen in the presence of SDS. The results show that SDS affects the conformation and thermal stability of collagen very differently depending on its concentrations. At CSDS ≤ 0.05 mM, the enhanced thermal stability of collagen indicates the stabilizing effect by SDS. However, a further increase of SDS leads to the denaturation of collagen, verifying the well-known ability of SDS to unfold proteins. This striking difference in thermodynamics and conformational changes of collagen caused by SDS concentrations can be explained in terms of their interactions. With increasing SDS, the binding of SDS to collagen can be dominated by electrostatic interaction shifting to hydrophobic interaction, and the latter plays a key role in loosening and unfolding the triple-helix structure of collagen. The important finding in the present study is the stabilizing effect of SDS on collagen molecules at extreme low concentration. Graphical abstract

Effect of GroEL on Thermal Aggregation of Glycogen Phosphorylase b from Rabbit Skeletal Muscle

2010 ◽  
Vol 10 (7) ◽  
pp. 768-774 ◽  
Author(s):  
Tatyana B. Eronina ◽  
Natalia A. Chebotareva ◽  
Svetlana G. Bazhina ◽  
Sergey Y. Kleymenov ◽  
Irina N. Naletova ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Glycogen Phosphorylase ◽  
Rabbit Skeletal Muscle ◽  
Thermal Aggregation ◽  
Glycogen Phosphorylase B

Thermal Stability of N-Heterocycle-Stabilized Iodanes – A Systematic Investigation

2019 ◽  
Author(s):  
Andreas Boelke ◽  
Yulia A. Vlasenko ◽  
Mekhman S. Yusubov ◽  
Boris Nachtsheim ◽  
Pavel Postnikov
Keyword(s):  
Thermal Stability ◽  
Differential Scanning Calorimetry ◽  
Thermogravimetric Analysis ◽  
Systematic Investigation ◽  
Scanning Calorimetry ◽  
Thermal Stability Of

<p>The thermal stability of pseudocyclic and cyclic <i>N</i>-heterocycle-stabilized (hydroxy)aryl- and mesityl(aryl)-l<sup>3</sup>-iodanes (NHIs) through thermogravimetric analysis (TGA) and differential scanning calorimetry (DSC) is investigated. NHIs bearing <i>N</i>-heterocycles with a high N/C-ratio such as triazoles show among the lowest descomposition temperatures and the highest decomposition energies. A comparison of NHIs with known (pseudo)cyclic benziodoxolones is made and we further correlated their thermal stability with reactivity in a model oxygenation. </p>

pH-Dependent Thermal Stability of Vibrio cholerae L-asparaginase

2019 ◽  
Vol 26 (10) ◽  
pp. 743-750 ◽  
Author(s):  
Remya Radha ◽  
Sathyanarayana N. Gummadi
Keyword(s):  
Vibrio Cholerae ◽  
Conformational Changes ◽  
Kinetic Studies ◽  
Structural Features ◽  
Structure Stability ◽  
Kcal Mole ◽  
Scanning Calorimetry ◽  
Wide Range ◽  
Ph Dependent ◽  
Ph Range

Background:pH is one of the decisive macromolecular properties of proteins that significantly affects enzyme structure, stability and reaction rate. Change in pH may protonate or deprotonate the side group of aminoacid residues in the protein, thereby resulting in changes in chemical and structural features. Hence studies on the kinetics of enzyme deactivation by pH are important for assessing the bio-functionality of industrial enzymes. L-asparaginase is one such important enzyme that has potent applications in cancer therapy and food industry.Objective:The objective of the study is to understand and analyze the influence of pH on deactivation and stability of Vibrio cholerae L-asparaginase.Methods:Kinetic studies were conducted to analyze the effect of pH on stability and deactivation of Vibrio cholerae L-asparaginase. Circular Dichroism (CD) and Differential Scanning Calorimetry (DSC) studies have been carried out to understand the pH-dependent conformational changes in the secondary structure of V. cholerae L-asparaginase.Results:The enzyme was found to be least stable at extreme acidic conditions (pH< 4.5) and exhibited a gradual increase in melting temperature from 40 to 81 °C within pH range of 4.0 to 7.0. Thermodynamic properties of protein were estimated and at pH 7.0 the protein exhibited ΔG37of 26.31 kcal mole-1, ΔH of 204.27 kcal mole-1 and ΔS of 574.06 cal mole-1 K-1.Conclusion:The stability and thermodynamic analysis revealed that V. cholerae L-asparaginase was highly stable over a wide range of pH, with the highest stability in the pH range of 5.0–7.0.

Mechanical and thermal characterization of grafted PP-NCC nanocomposites

2019 ◽  
pp. 089270571987822
Author(s):  
Saud Aldajah ◽  
Mohammad Y Al-Haik ◽  
Waseem Siddique ◽  
Mohammad M Kabir ◽  
Yousef Haik
Keyword(s):  
Thermal Properties ◽  
Interfacial Adhesion ◽  
Thermal Characterization ◽  
Mechanical And Thermal Properties ◽  
Screw Extruder ◽  
Scanning Calorimetry ◽  
Three Point Bending ◽  
Twin Screw ◽  
Thermal Stability Of

This study reveals the enhancement of mechanical and thermal properties of maleic anhydride-grafted polypropylene (PP- g-MA) with the addition of nanocrystalline cellulose (NCC). A nanocomposite was manufactured by blending various percentages of PP, MA, and NCC nanoparticles by means of a twin-screw extruder. The influence of varying the percentages of NCC on the mechanical and thermal behavior of the nanocomposite was studied by performing three-point bending, nanoindentation, differential scanning calorimetry (DSC), thermogravimetric analysis (TGA), scanning electron microscopy (SEM), and Fourier-transform infrared (FTIR) spectroscopy tests. The novelty of this study stems on the NCC nanoparticles and their ability to enhance the mechanical and thermal properties of PP. Three-point bending and nanoindentation tests revealed improvement in the mechanical properties in terms of strength, modulus, and hardness of the PP- g-MA nanocomposites as the addition of NCC increased. SEM showed homogeneity between the mixtures which proved the presence of interfacial adhesion between the PP- g-MA incorporated with NCC nanoparticles that was confirmed by the FTIR results. DSC and TGA measurements showed that the thermal stability of the nanocomposites was not compromised due to the addition of the coupling agent and reinforced nanoparticles.

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