Fourier Transform Infrared Spectroscopic Analysis of Protein Secondary Structures

Kong, Jilie; Yu, Shaoning

doi:10.1111/j.1745-7270.2007.00320.x

Cited by 2,882 publications

(1,989 citation statements)

References 49 publications

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“…Second derivative ATR FTIR spectra do not provide quantitative information for protein secondary structure, therefore, quantitative information was obtained by deconvolution of the FTIR spectra into Voigt‐shaped peaks. The peak area of individual amide I bands is correlated with secondary structure composition 41, 42, 43. The FTIR spectra were fitted with peaks centered at 1632 ± 3 cm −1 (β‐sheet), 1642 ± 3 cm −1 (random coil), 1657 ± 3 cm −1 (α‐helix), 1678 ± 4 cm −1 (β‐turn), and 1695 ± 4 cm −1 (β‐sheet).…”

Section: Resultsmentioning

confidence: 99%

Spectroscopic analysis of chlamydial major outer membrane protein in support of structure elucidation

et al. 2018

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Chlamydial major outer membrane protein (MOMP) is the major protein constituent of the bacterial pathogen Chlamydia trachomatis. Chlamydia trachomatis Serovars D–K are the leading cause of genital tract infections which can lead to infertility or ectopic pregnancies. A vaccine against Chlamydia is highly desirable but currently not available. MOMP accounts for ~ 60% of the chlamydial protein mass and is considered to be one of the lead vaccine candidates against C. trachomatis. We report on the spectroscopic analysis of C. trachomatis native MOMP Serovars D, E, F, and J as well as C. muridarum MOMP by size exclusion chromatography multi angle light scattering (SEC MALS), circular dichroism (CD) and attenuated total reflectance Fourier transform infrared spectroscopy (ATR‐FTIR). MOMP was purified from the native bacterium grown in either adherent HeLa cells or in different suspension cell lines. Our results confirm that MOMP forms homo‐trimers in detergent micelles. The secondary structure composition of C. trachomatis MOMP was conserved across serovars, but different from composition of C. muridarum MOMP with a 13% (CD) to 18% (ATR‐FTIR) reduction in β‐sheet conformation for C. trachomatis MOMP. When Serovar E MOMP was isolated from suspension cell lines the α‐helix content increased by 7% (CD) to 13% (ATIR‐FTIR). Maintenance of a native‐like tertiary and quaternary structure in subunit vaccines is important for the generation of protective antibodies. This biophysical characterization of MOMP presented here serves, in the absence of functional assays, as a method for monitoring the structural integrity of MOMP.

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Section: Resultsmentioning

confidence: 99%

Spectroscopic analysis of chlamydial major outer membrane protein in support of structure elucidation

et al. 2018

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“…Amide-B band was found at 3081-3082 cm -1 for both film samples. Amide-B band illustrated NH-stretching vibration and asymmetric CHstretching vibration (Kong and Yu 2007). Additionally, peaks at wavenumbers of 2930 and 2877 cm -1 for the control film were shifted to lower wavenumbers of 2923 and 2853 cm -1 when palm oil was incorporated.…”

Section: Fourier-transform Infrared (Ftir) Spectroscopymentioning

confidence: 93%

Influence of palm oil and glycerol on properties of fish skin gelatin-based films

2016

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Properties of fish skin gelatin film incorporated with palm oil at 50 and 75 % (w/w) as affected by glycerol at 0-30 % (w/w) were investigated. Increases in water vapour permeability and elongation at break along with decrease in tensile strength were noticed when levels of glycerol were increased (p \ 0.05). Decrease in L*-and a*-values with coincidental increase in b*-and DE*-values were observed in emulsified films when amount of palm oil incorporated increased (p \ 0.05). Light transmittance of all films increased as glycerol levels were increased (p \ 0.05). FTIR results suggested that the protein-protein interaction in film matrix decreased when palm oil was incorporated. Films added with palm oil had lower glass transition and degradation temperatures than control films. The addition of 75 % palm oil and 10 % glycerol improved water vapour barrier property of fish skin gelatin films without drastic alteration of mechanical properties.

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“…The region of the infrared spectrum between 1600 and 1700 cm -1 is assigned to the amide I vibration of the peptide backbone [46][47][48] . This amide I region corresponds to the C=O stretching vibration, which is directly related to the secondary structure of the protein backbone and is commonly used for the quantitative analysis of different secondary structures 49 . Annealed (EIS)x2 samples underwent a shift of the amide I band towards the 1600-1640 cm -1 region with respect to the control (unannealed (EIS)x2).…”

Section: Molecular Level: Ftir Analysismentioning

confidence: 99%

Self-Organized ECM-Mimetic Model Based on an Amphiphilic Multiblock Silk-Elastin-Like Corecombinamer with a Concomitant Dual Physical Gelation Process

et al. 2014

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ABSTRACT. Although significant progress has been made in the area of injectable hydrogels for biomedical applications and model cell niches, further improvements are still needed, especially in terms of mechanical performance, stability and biomimicry of the native fibrillar architecture found in the extracellular matrix (ECM). This work focuses on the design and production of a silk-elastin-based injectable multiblock co-recombinamer that spontaneously forms a stable physical nanofibrillar hydrogel under physiological conditions. That differs from previously reported silk-elastin-like polymers on a major content and predominance of the elastin-like part, as well as a more complex structure and behavior of such part of the molecule, which is aimed to obtain well defined hydrogels.Rheological and DSC experiments showed that this system displays a coordinated and concomitant dual gelation mechanism. In a first stage, a rapid, thermally driven gelation of the co-recombinamer solution takes place once the system reaches body temperature due to the thermal responsiveness of the elastinlike (EL) parts and the amphiphilic multiblock design of the co-recombinamer. A bridged micellar 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 2 structure is the dominant microscopic feature of this stage, as demonstrated by AFM and TEM.Completion of the initial stage triggers the second, which comprises a stabilization, reinforcement, and microstructuring of the gel. FTIR analysis shows that these events involve the formation of β-sheets around the silk motifs. The emergence of such β-sheet structures leads to the spontaneous selforganization of the gel into the final fibrous structure. Despite the absence of biological cues, here we set the basis of the minimal structure that is able to display such a set of physical properties and undergo microscopic transformation from a solution to a fibrous hydrogel. The results point to the potential of this system as a basis for the development of injectable fibrillar biomaterial platforms towards a fully functional, biomimetic, artificial extracellular matrix and cell niches.

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Fourier Transform Infrared Spectroscopic Analysis of Protein Secondary Structures

Cited by 2,882 publications

References 49 publications

Spectroscopic analysis of chlamydial major outer membrane protein in support of structure elucidation

Spectroscopic analysis of chlamydial major outer membrane protein in support of structure elucidation

Influence of palm oil and glycerol on properties of fish skin gelatin-based films

Self-Organized ECM-Mimetic Model Based on an Amphiphilic Multiblock Silk-Elastin-Like Corecombinamer with a Concomitant Dual Physical Gelation Process

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