Protein secondary structure content in solution, films and tissues: Redundancy and complementarity of the information content in circular dichroism, transmission and ATR FTIR spectra

Goormaghtigh, Erik; Gasper, Régis; Bénard, Audrey; Goldsztein, A.; Raussens, Vincent

doi:10.1016/j.bbapap.2009.06.007

Cited by 113 publications

(95 citation statements)

References 88 publications

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“…Second, the peaks may shift and change in intensity for purely optical reasons as explained in section 2.3. Goormaghtigh and coworkers dismiss the latter effect as insignificant for thin films, 175 but it still presents a potential complication for thicker films that could lead to the mis-assignment of secondary structures. The possibility of a protein denaturing on the ATR element is a more serious problem; however, if multilayers of protein are used the first layer-directly adsorbed to the surface-either contributes little to the overall spectrum or can be removed by spectral subtraction.…”

Section: Proteinsmentioning

confidence: 99%

“…ATR-IR offers the possibility to study a thin layer of protein deposited on an ATR element, which is appealing since the analysis uses only a tiny amount of protein 175 -∼10 ng compared to 10-100 µg in a 5 µm cell. 173 A further appealing property of ATR-IR is the reduction in path length of the water recorded.…”

Section: Proteinsmentioning

confidence: 99%

“…However, there are two important differences between transmission IR and ATR-IR spectra. 172,175 First, proteins in adsorbed films may be partially dehydrated which can affect the protein structure. Second, the peaks may shift and change in intensity for purely optical reasons as explained in section 2.3.…”

Section: Proteinsmentioning

confidence: 99%

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Total internal reflection spectroscopy for studying soft matter

Woods

Bain

2014

Soft Matter

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Total internal reflection (TIR) spectroscopy is a widely used technique to study soft matter at interfaces. This tutorial review aims to provide researchers with an overview of the principles, experimental design and applications of TIR spectroscopy to enable them to understand how this class of techniques might be used in their research. It also highlights limitations and pitfalls of TIR techniques, which will assist readers in critically analysing the literature. Techniques covered include attenuated total reflection infrared spectroscopy (ATR-IR), TIR fluorescence, TIR Raman scattering and cavity-enhanced techniques. Other related techniques are briefly described.

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Section: Proteinsmentioning

confidence: 99%

Section: Proteinsmentioning

confidence: 99%

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Total internal reflection spectroscopy for studying soft matter

Woods

Bain

2014

Soft Matter

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“…FTIR has been shown to be particularly sensitive to protein secondary structure based on the vibrational frequency of the amide I (C=O) band, which is affected by different hydrogen-bonding environments for α-helix, β-sheet, β-turn, and random coil (Miller and Dumas 2010). Until the nineties, the quality of FTIR increased gradually to reach extremely good signal-to-noise ratios (Goormaghtigh et al 2009). It was found that the newly advanced synchrotron technology (S-FTIR) as a rapid, direct, non-invasive, and non-destructive bio-analysis technique ( Wetzel et al 1998;Yu 2005a) could be used to reveal protein structures of feedstuff tissues affected by heat processing ( Yu 2005a;Doiron et al 2009) and investigate the relationship between protein molecular structures and protein degradation kinetics and nutritive value in the rumen ( Yu 2005b;Yu and Nuez-Ortin 2010).…”

mentioning

confidence: 99%

Effect of protein secondary structures in mixed feedstuff detected by Fourier transform infrared spectroscopy on ruminal protein degradation kinetics

Liu¹,

Li²,

Zhang³

et al. 2017

CZECH J ANIM SCI

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The objective of this study was to investigate the relationship between the protein secondary structure and the protein rumen degradation kinetics and the protein fractions of mixed feedstuffs of soybean meal with distillers dried grains with solubles (DDGS) at five mixed ratios (DDGS to soybean meal: 100 : 0, 70 : 30, 50 : 50, 30 : 70, 0 : 100). The Fourier transform infrared (FTIR) as a novel and cheap approach was used to detect the protein secondary structure, and the in situ nylon bag method was used to measure degradation kinetics of protein. Protein fractions were classified based on the Cornell net carbohydrate protein system. The results showed that (1) with the increasing soybean meal rate, the ruminal degraded protein and fractions of PB1 and PB2 were changed, (2) a higher α-helix to β-sheet ratio could result in a higher ruminally degraded protein, lower PB3 and PC, and higher PB1 and PB2 fractions in the feedstuff. So, mixing processing changed the feedstuff protein molecular structure spectral feature, which could influence the rumen degradation kinetics and protein fractions. It was inferred that protein degradation rate in mixed feedstuff can be measured by FTIR. There is an increasing need for protein structure evaluation and the studies on evaluating the protein nutritive values of feedstuff have become a global research focus. Protein is one of the most important nutrients in human and animal diet. Soybean meal and distillers dried grains with solubles (DDGS, co-product of fuel ethanol production) have high protein content and are mainly used as an important

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“…Furthermore, IR spectra account not only for the chemical nature of cell molecules but also for their conformation. They are in particular very sensitive to protein secondary structure [2,[8][9][10]12]. When coupled with a microscope device, this technique provides spatially resolved information on the sample.…”

Section: Introductionmentioning

confidence: 99%

Analysis of protein microarrays by FTIR imaging

Meutter

Derfoufi

Goormaghtigh

2016

BSI

Self Cite

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Abstract. BACKGROUND:Proteins are sensitive to environmental conditions. Whether they are produced for therapeutic purposes or for fundamental research, the integrity of their structure and post-traductional modifications are key issues. Measuring glycosylation or phosphorylation level as well as their secondary structure most often rely on complex and indirect experiments. Infrared spectroscopy presents a series of advantages related to its multivariate character. There is a lack of high-throughput methods able to analyse these parameters. OBJECTIVE: In this paper we attempted to combine protein microarrays and infrared imaging for high throughput analysis of proteins. METHODS: A protein microarrayer was used to produce protein microarrays on BaF 2 slides transparent in the mid-infrared. Spot density was about 25 spots/mm 2 . A 128 × 128 focal plane array infrared detector was used to record images of the protein microarrays. RESULTS: We show that 100 µm diameter spot are easily analyzed. Spots obtained with low protein concentrations, resulting in an average of a single protein monolayer (ca 3 fg/µm 2 for a 66 kDa protein) provided good quality spectra. CONCLUSIONS: Infrared imaging is a label free, high throughput method, able to analyse protein microarrays and to take advantage from the wide information available in the infrared spectra.

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Protein secondary structure content in solution, films and tissues: Redundancy and complementarity of the information content in circular dichroism, transmission and ATR FTIR spectra

Cited by 113 publications

References 88 publications

Total internal reflection spectroscopy for studying soft matter

Total internal reflection spectroscopy for studying soft matter

Effect of protein secondary structures in mixed feedstuff detected by Fourier transform infrared spectroscopy on ruminal protein degradation kinetics

Analysis of protein microarrays by FTIR imaging

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