Thermodynamic Effects of Disulfide Bond on Thermal Unfolding of the Starch-Binding Domain of Aspergillus niger Glucoamylase

@article{Sugimoto2007ThermodynamicEO,
  title={Thermodynamic Effects of Disulfide Bond on Thermal Unfolding of the Starch-Binding Domain of Aspergillus niger Glucoamylase},
  author={Hayuki Sugimoto and Miho Nakaura and Yoshie Kosuge and Kunio Imai and Hideo Miyake and S Karita and Akiyoshi Tanaka},
  journal={Bioscience, Biotechnology, and Biochemistry},
  year={2007},
  volume={71},
  pages={1535 - 1541}
}
The thermodynamic effects of the disulfide bond of the fragment protein of the starch-binding domain of Aspergillus niger glucoamylase was investigated by measuring the thermal unfolding of the wild-type protein and its two mutant forms, Cys3Gly/Cys98Gly and Cys3Ser/Cys98Ser. The circular dichroism spectra and the thermodynamic parameters of binding with β-cyclodextrin at 25 °C suggested that the native structures of the three proteins are essentially the same. Differential scanning calorimetry… Expand
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References

SHOWING 1-10 OF 37 REFERENCES
Thermal unfolding of the starch binding domain of Aspergillus niger glucoamylase.
A fragment of the starch-binding domain (SBDF) of Aspergillus niger glucoamylase was prepared using recombinant DNA techniques, and its thermal unfolding was investigated by high-sensitivityExpand
Mechanism of protein stabilization by disulfide bridges: calorimetric unfolding studies on disulfide-deficient mutants of the alpha-amylase inhibitor tendamistat.
TLDR
Two disulfide bridge mutants of the alpha-amylase inhibitor Tendamistat where the large loop or the small loop had been opened by recombinant DNA techniques are investigated, and the stability of the mutated proteins with that of wild-type Tendamists published previously is compared. Expand
Thermodynamic effects of reduction of the active-site disulfide of Escherichia coli thioredoxin explored by differential scanning calorimetry.
TLDR
The active site of Escherichia coli thioredoxin possesses a disulfide/dithiol in a short loop, oxidation/reduction of which is accompanied by little structural alteration of the protein, and data for the thermal denaturation of the reduced protein are presented. Expand
Enthalpic destabilization of a mutant human lysozyme lacking a disulfide bridge between cysteine-77 and cysteine-95.
TLDR
Although X-ray crystallography indicated that the mutants preserve the wild-type tertiary structure, removal of the disulfide bridge increased the flexibility of the native state of the mutants, and the effect of cross-linking on the stability of a protein is not solely explained by the entropy change in denaturation. Expand
Enthalpic and entropic contributions mediate the role of disulfide bonds on the conformational stability of Interleukin‐4
TLDR
Analysis of the role of disulfide bridges in IL4 reveals that both mutant proteins have lower conformational stability than the wild‐type protein and plays a critical role in maintaining the thermodynamic stability and core packing of the helix bundle. Expand
Disulfide bond effects on protein stability: Designed variants of Cucurbita maxima trypsin inhibitor‐V
TLDR
Overall, the results show that an enthalpy‐entropy compensation accompanies disulfide bond effects and protein stabilization is profoundly modulated by altered hydrophobicity of both native and denatured states, altered flexibility near the cross‐link, and residual structure in theDenatured state. Expand
Effects of the difference in the unfolded-state ensemble on the folding of Escherichia coli dihydrofolate reductase.
TLDR
The structure, stability, and folding of "circular" dihydrofolate reductase (DHFR) from Escherichia coli in which the N and C-terminal regions are cross-linked by a disulfide bond is studied, and the results suggest that Circular DHFR is more stable than linear DHFR, which may be due to the decrease in the conformational entropy of the unfolded state as a result of circularization. Expand
Differential scanning calorimetric studies on the domain structure of Aspergillus glucoamylase.
TLDR
The thermal unfolding of the starch-binding domain was found to be reversible, but that of the catalytic domain was irreversible. Expand
"Designing out" disulfide bonds: thermodynamic properties of 30-51 cystine substitution mutants of bovine pancreatic trypsin inhibitor.
TLDR
Analysis of denaturation transitions for a family of mutants suggests that a previously unrecognized component of disulfide bridge stabilization of proteins is the relatively minor penalty in side chain conformational entropy incurred by cystine residues during folding due to their severely restricted rotation even in the unfolded state. Expand
Crystal structure of the disulfide bond-deficient azurin mutant C3A/C26A: how important is the S-S bond for folding and stability?
TLDR
The rate of unfolding for the C3A/C26A mutant is similar to that of the wild-type protein, suggesting that the site of the mutation is not involved in an early unfolding reaction. Expand
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