Temperature induced structural transitions from native to unfolded aggregated states of tobacco etch virus protease

Zhu, Gangjie; Ren, Siyan; Xi, Lei; Du, Linfang; Zhu, Xiaofeng

doi:10.1016/j.molstruc.2014.11.010

Cited by 12 publications

(10 citation statements)

References 54 publications

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“…T m , a criterion for the thermostability, defined as the midpoint of the denaturation process 11,23 , was summarized in Table 1. On the one hand, the T m values of Pin1-WT, H59R and H157R were similar when the temperature was between 20 and 60 °C, indicating that the influence of histidine mutations to structural stability was not sensitive below 60 °C.…”

Section: Resultsmentioning

confidence: 99%

“…The far-UV CD spectra can provide accurately the information of secondary structure 11,19,23 . The representative far-UV CD signal of Pin1-WT showed in Fig.…”

Section: Resultsmentioning

confidence: 99%

“…In the unfolding studies, the fraction of Pin1-WT and mutants at each temperature was calculated using the following equation 11,19 :where f u is the fraction of unfolded Pin1-WT and mutants at a given temperature, F obs is the fluorescence intensity or CD signal intensity at the temperature, F n and F d are the fluorescence intensity or CD signal intensity of the native and denatured protein, respectively. T m , a temperature of the denaturation process at the midpoint, was calculated by the plotting f u against temperature 11,23,49 .…”

Section: Methodsmentioning

confidence: 99%

“…K eq is the fraction of unfolded protein at each temperature. The apparent Gibbs free energy ( ΔG u ) is related to the free energy of unfolding by the following equation 23,51 :where m is the experimental measure of the dependence of ΔG u on temperature.…”

Section: Methodsmentioning

confidence: 99%

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Insight into the structural stability of wild-type and histidine mutants in Pin1 by experimental and computational methods

Wang

Xiong

et al. 2019

Sci Rep

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Pin1, a polypeptide proline isomerase parvulin, plays a key role in Alzheimer’s disease (AD), common tumors and cancers. Two conservative histidine residues, His59 and His157, are important for maintaining the stability of the PPIase domain. Hence multiple spectral and computational techniques were performed to investigate the potential mechanism of two histidine residues. Thermal denaturation indicated that both residues His59 and His157 are not sensitive to the lower temperatures, while residue His59 is more sensitive to the higher temperatures than residue His157. Acidic denaturation suggested that influences of both residues His59 and His157 to acidic stability were the difference from Pin1-WT. ANS and RLS spectra hinted that there was no significant effect on hydrophobic change and aggregation by histidine mutations. The GndHCl-induced denaturation implied that residues His59 and His157 contributed the most to the chemical stability. MD simulations revealed that residues His59 and His157 mutations resulted in that the hydrogen bond network of the dual histidine motif was destroyed wholly. In summary, these histidine residues play an important role in maintaining the structural stability of the PPIase domain.

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Section: Resultsmentioning

confidence: 99%

“…The far-UV CD spectra can provide accurately the information of secondary structure 11,19,23 . The representative far-UV CD signal of Pin1-WT showed in Fig.…”

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 2 more Smart Citations

Insight into the structural stability of wild-type and histidine mutants in Pin1 by experimental and computational methods

Wang

Xiong

et al. 2019

Sci Rep

Self Cite

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“…It can be seen that the intensity goes up and then down in the temperature from 30 to 85 C and reaches a maximum at 55 C. This may be a proof of the existence of an intermediate state between the native and fully unfolded structure, which has been reported in the literature. 40 The folding or unfolding of large globular proteins is often characterized by the formation of intermediates owning partial native structure of protein. Therefore, the temperature-induced structural change of HSA seems to occur through a two-step process of at least two transitions with a stable intermediate state.…”

Section: Structural Changes Of Hsa In Aqueous Solution With Temperaturementioning

confidence: 99%

Investigating the Structural Change in Protein Aqueous Solution Using Temperature-Dependent Near-Infrared Spectroscopy and Continuous Wavelet Transform

Cai

Shao

2016

Appl Spectrosc

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The circulatory protein, human serum albumin (HSA), is widely used as a model protein for the study of protein structure. In this work, the structures of human serum albumin in aqueous solutions are studied using temperature-dependent near-infrared (NIR) spectroscopy with the aid of continuous wavelet transform (CWT). Near-infrared spectra of human serum albumin solutions with different concentrations were measured over a temperature range of 30-85 ℃. Then, continuous wavelet transform was performed on the spectra to enhance the resolution. As a result of the resolution enhancement, spectral bands around 4361, 4521, 4600 and 4260 cm were extracted from the overlapping low-resolution signals. The four bands can be assigned to the protein structures of α-helix, β-sheet, an intermediate state and side chains, respectively. The variations in intensity of the bands around 4361 and 4521 cm with temperature show that the increase of temperature leads to the loss of α-helical structure but the formation of β-sheet, and the denaturation temperature of human serum albumin is about 55 ℃. The variation of the band around 4600 cm indicates that the temperature-induced unfolding process of human serum albumin occurs through a stable intermediate state, and a significant change in the microenvironment of the side chains about 63 ℃ is observed from the variation of the band around 4260 cm. On the other hand, the transformed spectra in the region of 8000-5600 cm provide an explicit evidence for the structural changes of water during the process of protein denaturation, and the unfolding process of HSA can be reflected by these changes.

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Effects of temperature and pH on the structure of a metalloprotease from Lactobacillus fermentumR6 isolated from Harbin dry sausages and molecular docking between protease and meat protein

et al. 2021

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BACKGROUND Microbial protease can interact with meat protein in fermented meat products at a certain pH and temperature. To investigate the effects of various pH values and temperatures on the structural characteristics of Lactobacillus fermentum R6 protease, which was isolated from Harbin dry sausages, spectroscopy techniques and molecular dynamics were utilized to evaluate structural changes. RESULTS The protease exhibited a stable spatial structure at pH 7 and 40 °C, and the extension of the protease structure was also promoted. Although the structure of the protease could be changed or destroyed by pH 8 and 70 °C, it was mainly determined by the changes of secondary and tertiary structures such as α‐helix, β‐sheet, β‐turn and random coil. In addition, carbonyl vibration, ‐NH vibration, C–H stretching vibration and disulphide bonds were present in L. fermentum R6 protease under various pH and temperature conditions. Molecular docking showed that the protease can interact with myosin light chain, myosin heavy chain, actin and myoglobin. CONCLUSION The protease can maintain stable structure and interact with meat protein, which reflected certain application prospects in the fermentation of Harbin dry sausages. © 2021 Society of Chemical Industry

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Temperature induced structural transitions from native to unfolded aggregated states of tobacco etch virus protease

Cited by 12 publications

References 54 publications

Insight into the structural stability of wild-type and histidine mutants in Pin1 by experimental and computational methods

Insight into the structural stability of wild-type and histidine mutants in Pin1 by experimental and computational methods

Investigating the Structural Change in Protein Aqueous Solution Using Temperature-Dependent Near-Infrared Spectroscopy and Continuous Wavelet Transform

Effects of temperature and pH on the structure of a metalloprotease from Lactobacillus fermentumR6 isolated from Harbin dry sausages and molecular docking between protease and meat protein

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