Fast determination of the quantitative secondary structure of proteins by using some parameters of the Raman Amide I band

Alix, Alain J. P.; Pedanou, G.; Berjot, M.

doi:10.1016/0022-2860(88)80151-0

Cited by 267 publications

(174 citation statements)

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“…Herman, Adams, & Howell, 2004). Thus, quantitative information about secondary structure of meat protein could be estimated from the amide I spectral profile (Alix et al, 1988). According to Table 4, there were significant effects (P < 0.05) of MTGase on the values of secondary structural percentages content in frankfurters, mainly decreased α-helices and increased β-sheet, β-turn, which is consistent with the amide I spectral changes (Figure 2).…”

Section: Changes Of Secondary Structuressupporting

confidence: 67%

“…Yvon, Long-jumeau, France). The secondary structures of the proteins were determined as percentages of α-helix, β-sheet, β-turn and random coil or unordered conformations (Alix, Pedanou, & Berjot, 1988). With this aim, the water spectrum was subtracted from the spectra by following the same criteria as that described previously (Alix et al, 1988;Herrero, Carmona, Pintado, Jiménez-Colmenero, & Ruíz-Capillas, 2011).…”

Section: Raman Spectroscopicmentioning

confidence: 99%

“…This Raman band could provide secondary structural information about protein (Alix et al, 1988;Herrero, 2008;Tu, 1982), which involves mainly C=O stretching and to lesser degrees C-N stretching, Cα-C-N bending and N-H in-plane bending of peptide groups. Raman spectra (Figure 2) showed a slight shift from 1658 cm −1 to higher frequencies of the maximum intensity of this band (1660, 1661 and 1661 cm −1 ) after MTGase was added to frankfurters, indicating a reduction in the α-helical structure.…”

Section: Changes Of Secondary Structuresmentioning

confidence: 99%

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Effect of the levels of transglutaminase in frankfurters: a physical–chemical and Raman spectroscopy study

Kang

2016

CyTA - Journal of Food

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Microbial transglutaminase (MTGase) is a kind of enzyme preparation which is used in the processing of emulsified meat products for improving the quality. In this paper, the effect of MTGase content on water-holding capacity, texture and protein structure was studied by using Raman spectroscopy. The results showed that emulsion stability and cooking yield were significantly (P < 0.05) improved with increased MTGase content. But when the contents were 0.67% and 1%, the emulsion stability and cooking yield had no significant difference (P > 0.05). The hardness, springiness, cohesiveness and chewiness also were significantly (P < 0.05) improved with increased MTGase content. The result of Raman spectroscopy found that the wave peak of amide I shifted from 1658 to 1660, 1661 and 1661 cm −1 when added various amounts of MTGase, β-sheet and β-turn contents were significantly (P < 0.05) increased with decreased α-helix content, and random coil was not a significant difference (P > 0.05); the wave peak of 3100-3500 cm −1 shifted from 3226 to 3228, 3229 and 3229 cm −1 that indicated OH stretching motions were stronger. Overall, when added appropriately, MTGase to frankfurters could change the protein conformation, improve the texture and water-holding capacity.Efecto de los niveles de transglutaminasa en las salchichas Frankfurt: Un estudio fisicoquímico y espectroscopia Raman RESUMEN La transglutaminasa microbial (MTGase) es un tipo de preparado encimático utilizado en el procesamiento de productos cárnicos emulsionados para mejorar su calidad. En este estudio se ha investigado el efecto del contenido de MTGase en la capacidad de retención de agua, la textura y la estructura proteínica mediante la utilización de espectroscopia Raman. Los resultados mostraron que la estabilidad de emulsión y el rendimiento de cocinado mejoraron significativamente (P < 0,05) con el aumento del contenido de MTGase. Sin embargo, cuando los contenidos fueron 0,67% y 1%, la estabilidad de emulsión y el rendimiento de cocinado no obtuvieron diferencias significativas (P > 0,05). La dureza, la ligereza, la cohesión y la masticabilidad también fueron mejorados significativamente (P < 0,05) con el aumentó en el contenido de MTGase. Los resultados de la espectroscopia Raman indicaron que la ola pico de amida I cambió de 1658 cm −1 a 1660 cm, 1661 cm −y y 1661 cm −1 cuando fueron añadidas diferentes cantidades de Migase. Los contenidos de lámina β y giro β aumentaron significativamente (P < 0,05) cuando el contenido de hélice α disminuyó, además el movimiento aleatorio no fue significativamente diferente (P > 0,05); la ola pico de 3100-3500 cm , lo cual indicó que los movimientos de elasticidad de OH eran más fuertes. En general, la adición apropiada de MTGase a las salchichas Frankfurt podría cambiar la conformación proteínica, mejorar la textura y la capacidad de retención de agua. ARTICLE HISTORY

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Section: Changes Of Secondary Structuressupporting

confidence: 67%

Section: Raman Spectroscopicmentioning

confidence: 99%

Section: Changes Of Secondary Structuresmentioning

confidence: 99%

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Effect of the levels of transglutaminase in frankfurters: a physical–chemical and Raman spectroscopy study

Kang

2016

CyTA - Journal of Food

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“…The evaluation of the conformational changes of RNAse A upon irradiation was obtained by the Amide I analysis by two methods, one based on a combination of X-ray and Raman data base and the other involving the deconvolution of the spectral range of interest into component bands [8,9]. A similar trend of conformational changes was obtained by both methods (Table 1).…”

Section: Resultsmentioning

confidence: 85%

Structural lesion to ribonuclease A caused by reductive stress: Assessment by Raman spectroscopy

Torreggiani

2008

Spectroscopy

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Abstract. The damages induced by reductive radical stress on bovine pancreatic ribonuclease A (RNAse A) were investigated by Raman spectroscopy. Gamma-irradiation was used to simulate the endogenous formation of reductive species, in particular • H atom that is a simple one-electron equivalent reducing agent. Specific damages occur at sensitive amino acid sites, selectively, rather than indiscriminately, leading to the structure modification of the protein. Sulfur-containing residues (Met and Cys) and aromatic residues are appreciably attacked. In particular, extensive changes in the disulfide bridge conformations are induced as well as conformational changes of the protein secondary structure; a gradual conversion of α-helical to pleated-sheet geometry was evidenced, indicating a higher ability of reducing radicals in denaturing the protein structure compared with that of oxidizing radical species.

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“…Another source of ambiguity poses the assignment of the fitted Gaussian peaks to individual secondary structural elements. Overlapping spectral contributions to the amide I band in the Raman spectra have for example been described for -sheet and -turn structures [43]. Specifically for the amide I band in IR spectra of mammalian MTs it was shown that contributions usually assigned to -helical structures, i.e.…”

Section: >> Insertmentioning

confidence: 99%

Structural features specific to plant metallothioneins

Freisinger

2011

J Biol Inorg Chem

112

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The metallothionein (MT) superfamily combines a large variety of small cysteine-rich proteins from nearly all phyla of life that have the ability to coordinate various transition metal ions, including Zn(II), Cd(II), and Cu(I). The members of the plant MT family are characterized by great sequence diversity, requiring further subdivision into four subfamilies. Very peculiar and not well understood is the presence of rather long cysteine-free amino acid linkers between the cysteine-rich regions. In light of the distinct differences in sequence to MTs from other families, it seems obvious to assume that these differences will also be manifested on the structural level. This was already impressively demonstrated with the elucidation of the three-dimensional structure of the wheat E(c)-1 MT, which revealed two metal cluster arrangements previously unprecedented for any MT. However, as this structure is so far the only one available for the plant MT family, other sources of information are in high demand. In this review the focus is thus set on any structural features known, deduced, or assumed for the plant MT proteins. This includes the determination of secondary structural elements by circular dichroism, IR, and Raman spectroscopy, the analysis of the influence of the long linker regions, and the evaluation of the spatial arrangement of the sequence separated cysteine-rich regions with the aid of, e.g., limited proteolytic digestion. In addition, special attention is paid to the contents of divalent metal ions as the metal ion to cysteine ratios are important for predicting and understanding possible metal-thiolate cluster structures. Very peculiar and not well understood is the presence of rather long Cys-free amino acid linkers between the Cys-rich regions. In light of the distinct differences in sequence to MTs from other families it seems obvious to assume that these differences will be also manifested on the structural level. This was already impressively demonstrated with the elucidation of the three-dimensional structure of the wheat E c -1 MT, which revealed two metal cluster arrangements previously unprecedented for any MT. However, as this structure is so far the only one available for the plant MT family other sources of information are of high demand.In this review the focus is thus set on any structural features known, deduced or assumed for the plant MT proteins. This includes the determination of secondary structural elements by CD, IR, and Raman spectroscopy, the analysis of the influence of the long linker regions, as well as the evaluation of the spatial arrangement of the sequence separated Cys-rich regions with the aid of e.g. limited proteolytic digestion. In addition, special attention is paid to the contents of divalent metal ions as the metal ion-to-Cys ratios are important for predicting and

show abstract

Fast determination of the quantitative secondary structure of proteins by using some parameters of the Raman Amide I band

Cited by 267 publications

References 3 publications

Effect of the levels of transglutaminase in frankfurters: a physical–chemical and Raman spectroscopy study

Effect of the levels of transglutaminase in frankfurters: a physical–chemical and Raman spectroscopy study

Structural lesion to ribonuclease A caused by reductive stress: Assessment by Raman spectroscopy

Structural features specific to plant metallothioneins

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