The effect of disulfide bonds on protein folding, unfolding, and misfolding investigated by FT–Raman spectroscopy

Wang, Chih‐Hsien; Huang, Chün-chieh; Lin, Long-Liu; Chen, Wenlung

doi:10.1002/jrs.4935

Cited by 42 publications

(31 citation statements)

References 51 publications

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“…Processing treatments such as salting or cooking all assist in the changes of secondary and tertiary structure of proteins. Determining the structures of various proteins would aid in our understanding of the mechanisms of protein functions and of the changes of proteins digestibility (Wang, Huang, Lin, & Chen, 2016). Disulfide bonds stabilize the tertiary structure of proteins; 500-550 cm −1 are usually assigned to the S-S stretching vibrations of disulfide bonds, which are formed between the cystine of proteins (Brandt et al, 2008).…”

Section: Evaluating Protein Tertiary Structure By the Normalized Intementioning

confidence: 99%

“…Disulfide bonds stabilize the tertiary structure of proteins; 500-550 cm −1 are usually assigned to the S-S stretching vibrations of disulfide bonds, which are formed between the cystine of proteins (Brandt et al, 2008). Band located at 530 cm −1 has been assigned to disulfide bonds in the gauche-gauche-trans (Wang et al, 2016). Interestingly, the intensity of S-S at 530 cm −1 significantly decreased from the raw to 120°C, which could be explained that cooking temperatures caused the transformation from gauche-gauche-trans conformation to all-gauche and trans- Figure 3.…”

Section: Evaluating Protein Tertiary Structure By the Normalized Intementioning

confidence: 99%

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Evaluation of the secondary structure and digestibility of myofibrillar proteins in cooked ham

Zhou

Cao

Zhuang

et al. 2019

CyTA - Journal of Food

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The present study aimed to evaluate structure and digestibility of dry-cured ham in relation to different cooking temperatures (70, 100 and 120°C), and further assess the relationship between structure and digestibility. The secondary structure analysis showed that the content of α-helix decreased from 55.03% to 20.61%, accompanied by an increase in the content of β-sheet and random coil from the raw to 120°C. The digestibility showed that proteolysis rate of myofibrillar proteins by pepsin and trypsin & αchymotrypsin (digestive enzymes) significantly increased to 0.62 and 0.51 at 100°C, compared with the raw. Odour and taste were susceptible to cooking temperature, and 100°C enhanced odour and taste attributes of ham. The changes of protein conformation were closely related to the digestibility. Correlation analysis further demonstrated that activities of digestive enzymes for proteins were negatively correlated with α-helical and β-sheet, and positively correlated with β-turn and random coil. Evaluación de la estructura secundaria y la digestibilidad de las proteínas miofibrilares en el jamón cocido RESUMEN El presente estudio se propuso evaluar la estructura y la digestibilidad del jamón curado en seco a distintas temperaturas de cocción (70, 100 y 120°C), así como investigar la relación entre estructura y digestibilidad. El análisis de la estructura secundaria mostró que durante el proceso de elevación de la temperatura del jamón crudo a 120°C, el contenido de hélice-α disminuyó de 55.03% a 20.61%. Esto se acompañó de un aumento del contenido de lámina-β y espiral aleatoria. El análisis de la digestibilidad indicó que, en comparación con el jamón crudo, a 100°C la tasa de proteólisis de las proteínas miofibrilares aumentó a 0.62 y 0.51 a causa de la pepsina y tripsina & α-quimotripsina (enzimas digestivas), respectivamente. Tanto el olor como el sabor del jamón son susceptibles a la temperatura de cocción: una temperatura de 100°C mejoró los atributos de olor y de sabor del jamón. Los cambios en la conformación proteica se relacionan estrechamente con la digestibilidad. Además, el análisis de correlación demostró que las actividades de las enzimas digestivas en términos de proteínas se correlacionan negativamente con la hélice-α y la lámina-β, y positivamente con el giro-β y la espiral aleatoria.

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Section: Evaluating Protein Tertiary Structure By the Normalized Intementioning

confidence: 99%

Section: Evaluating Protein Tertiary Structure By the Normalized Intementioning

confidence: 99%

Evaluation of the secondary structure and digestibility of myofibrillar proteins in cooked ham

Zhou

Cao

Zhuang

et al. 2019

CyTA - Journal of Food

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“…The fitted peak areas of Raman spectroscopy at 500–510 cm −1 , 516–530 cm −1 and 535–545 cm −1 were used to indicate the content of gauche‐gauche‐gauche (g‐g‐g), trans‐gauche‐gauche (t‐g‐g) and trans‐gauche‐trans (t‐g‐t) conformations of disulfide bonds . The percentage of each peak area to the total peak area was used to indicate the percentage of each conformation, and is shown in Table .…”

Section: Resultsmentioning

confidence: 99%

“…The fitted peak areas of Raman spectroscopy at 500-510 cm −1 , 516-530 cm −1 and 535-545 cm −1 were used to indicate the content of gauche-gauche-gauche (g-g-g), trans-gauche-gauche (t-g-g) and trans-gauche-trans (t-g-t) conformations of disulfide bonds. 20,36 The percentage of each peak area to the total peak area was used to indicate the percentage of each conformation, and is shown in Table 2. The percentage of g-g-g and t-g-t conformations of disulfide bond decreased significantly (P < 0.05) as the HSH speed increased, whereas the t-g-g conformation significantly increased.…”

Section: Tertiary and Quaternary Structurementioning

confidence: 99%

Effects of high‐speed shear homogenization on the emulsifying and structural properties of myofibrillar protein under low‐fat conditions

et al. 2019

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BACKGROUND Emulsification is important for food quality and processing functionality. Most emulsification occurs under high‐fat conditions that eventually cause health concerns. Protein emulsifiers also have drawbacks such as lower dispersity. This study considered the effects of different high‐speed shear homogenization (HSH) speeds on the emulsifying and structural properties of myofibrillar proteins (MPs) under low‐fat conditions. RESULTS High‐speed shear homogenization significantly increased the emulsifying activity and emulsifying stability of MPs at lower speeds (8000 to 14 500 rpm). The primary structure of MP was not altered significantly by HSH, whereas its secondary, tertiary, and quaternary structures were changed. Particle size decreased first and then increased significantly, and reached a minimum when the HSH speed was 14 500 rpm. The absolute zeta potential values increased significantly and the dendritic fibrous structure of sample was destroyed when the speed exceeded 14 500 rpm. High‐speed shear homogenization (14 500 rpm) decreased the particle size and unfolded the protein, which improved the emulsifying properties of MPs. Excessive HSH speeds (20 500 rpm or higher) caused an aggregation of MP molecules, which was not conducive to improving their emulsifying properties. CONCLUSION Optimal HSH speed was achieved at 14 500 rpm to modify MPs' emulsifying and structural properties under low‐fatconditions. © 2019 Society of Chemical Industry

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“…They found that both disulfide bonds and secondary structure (mostly in α‐helix) of BSA appeared relatively stable even when the protein was unfolded by urea solution. However, disulfide bonds were completely reduced, and protein secondary structure changed from α‐helix to a relatively β‐sheet dominant structure when the protein was modified by the mixed solution of urea and dithiothreitol (urea/DTT) …”

Section: Biosciencesmentioning

confidence: 99%

Recent advances in linear and non‐linear Raman spectroscopy. Part XI

Nafie

2017

J Raman Spectroscopy

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This review, published annually, provides an overview of advances in the field of Raman spectroscopy as found in papers published in the preceding calendar year in the Journal of Raman Spectroscopy (JRS), as well as in trends over the past decade across journals that have published papers important to the field of Raman spectroscopy. This information is obtained from statistical data on article counts obtained from Clarivate Analytics' Web of Science Core Collection by year and by subfield of Raman spectroscopy. Additional information is gleaned from presentations at the IX International Conference on Advanced Vibrational Spectroscopy (ICAVS‐9) in Victoria, British Columbia, Canada, in June 2017 and those featuring Raman scattering at SCIX 2017 organized by the Federation of Analytical Chemistry and Spectroscopy Societies (FACSS) in Reno, Nevada, USA, in October 2017. Coverage is also provided for topics from the European Conference on Non‐linear Optical Spectroscopy (ECONOS 2017) held in April 2017 in Jena, Germany, and the Ninth Congress on the Application of Raman in Art and Archaeology (RAA 2017) in October 2017 in Evora, Portugal. Finally, papers published in JRS in 2016 are highlighted and arranged by topics at the frontier of Raman spectroscopy. Based on this survey information, it is clear that Raman spectroscopy maintains a rapidly expanding influence across a wide range of novel disciplines and applications that provide sensitive photonic information of matter at the molecular level.

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The effect of disulfide bonds on protein folding, unfolding, and misfolding investigated by FT–Raman spectroscopy

Cited by 42 publications

References 51 publications

Evaluation of the secondary structure and digestibility of myofibrillar proteins in cooked ham

Evaluation of the secondary structure and digestibility of myofibrillar proteins in cooked ham

Effects of high‐speed shear homogenization on the emulsifying and structural properties of myofibrillar protein under low‐fat conditions

Recent advances in linear and non‐linear Raman spectroscopy. Part XI

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