Analysis of Polypeptide and Protein Structures Using Fourier Transform Infared Spectroscopy

Haris, Parvez I.; Chapman, D.

doi:10.1385/0-89603-232-9:183

Cited by 47 publications

(59 citation statements)

References 29 publications

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“…Moreover, type II might be further subdivided into two sub-groups, one with weak peak intensity at 781 cm −1 (d-f ) and another with strong one (g-i). The specific IR spectral peaks at 1645 and 1642 cm −1 were assigned to the amide I band of protein [21,24]. The C-O bending vibration (ν 2 ) at about 872 (871) cm −1 and the C-O stretching (ν 3 ) at around 1417 cm −1 were the characteristic bands of carbonate in HA, respectively [19,39].…”

Section: Compositional Components Of Calcified Deposits In Prostatic mentioning

confidence: 97%

“…It is evident that all the FT-IR spectra shown in Figs 3 and 4 were similar, indicating similar compositions were produced at different positions in tendon samples. Several IR peaks near 1651 or 1654 (amide I of protein), 1450 or 1449 (CH 2 /CH 3 bending of lipid or amide III of protein), 1417 (carbonate), 1034 (ν 3 phosphate stretching), 959 (ν 1 phosphate stretching) and 873 (ν 2 carbonate mode) cm −1 were observed [3,5,17,21,22,24,29]. The appearance of IR peaks at 1034, and 959 cm −1 was similar to that of the IR spectrum of HA, indicating the calcified deposit predominantly consisted of HA [3,17,29].…”

Section: Compositional Components Of Calcified Deposits In Calcific Tmentioning

confidence: 99%

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Infrared microspectroscopic imaging as a probing tool to fast distinguish chemical compositions in calcified deposits of prostatic calculi and calcific tendonitis

Lin

Chiou

et al. 2011

Spectroscopy

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Abstract. The specificity and homogeneity of the real compositional components within the calcified deposits of prostatic calculi and calcific tendonitis were investigated using Fourier transform infrared (FT-IR) microspectroscopy with or without automatic imaging system. The second-derivative analysis was also applied to differentiate the overlapping components of individual spectra for the calcified samples. The FT-IR microscopic imaging results of present study indicate that the complicated components such as protein, type B or type A carbonated apatite, brushite and calcium oxalate monohydrate were contained in the calcified tissue of prostatic tissue, but the protein, type A and type B carbonated apatites were mainly included in the calcific tendonitis. However, the traditional manually single-point FT-IR spectral result only reveals a little component contained in the calcified tissues, leading to an inaccurate diagnose of the complicated components in the calcified mixture.

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Section: Compositional Components Of Calcified Deposits In Prostatic mentioning

confidence: 97%

Section: Compositional Components Of Calcified Deposits In Calcific Tmentioning

confidence: 99%

Infrared microspectroscopic imaging as a probing tool to fast distinguish chemical compositions in calcified deposits of prostatic calculi and calcific tendonitis

Lin

Chiou

et al. 2011

Spectroscopy

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“…1C). Indeed, the second derivative analysis of the protein Amide I band [10][11][12] allows determining the protein secondary structure, since Amide I is a structure sensitive band, being mainly due to the absorption of the carbonyl C‚O group of the peptide bond. Interestingly, it has been shown that the analysis of the Amide I band components enables also the detection of protein aggregates [4,6,7,13], which are not easily monitored by other optical spectroscopies.…”

Section: Detection Of Inclusion Bodies In Vivo By Ft-ir Spectroscopymentioning

confidence: 99%

Kinetics of inclusion body formation studied in intact cells by FT‐IR spectroscopy

et al. 2005

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The aggregation of a recombinant lipase as inclusion bodies (IBs) was studied directly within intact Escherichia coli cells by FT-IR microspectroscopy. Through this approach, it was possible to monitor in real time the different kinetics of IB formation at 37 and 27°C, in excellent agreement with the results of the SDS-PAGE analysis. Furthermore, insights on the residual native-like structure of the expressed protein within IB -both isolated and inside cells -were obtained by the secondary structure analysis of the Amide I band in the IB FT-IR spectra.

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“…The peaks at 1407-1409 cm −1 were due to the symmetric COO − stretching band and/or the deformation of CH 2 and CH 3 . The shoulders at 1081-1083 cm −1 were mainly corresponded to the contributions of C-O and C-N stretching modes [3,5]. Because all samples exhibited the similar IR spectra, suggesting that four sample preparation methods did not markedly alter the conformational structure of sCT in the solid state.…”

Section: Resultsmentioning

confidence: 90%

Different solid sample preparation methods affecting the spectral similarity of salmon calcitonin

Lin

Lee

2010

Spectroscopy

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Abstract. Salmon calcitonin (sCT) was selected as a model protein drug for investigating its structural similarity in the solid state by four sample preparation methods, such as tape, smeared, CaF 2 and film methods. The conformational changes of sCT in the solid state were estimated by using a second-derivative Fourier transform infrared (FT-IR) microspectroscopy. The tape method was acted as a standard reference.The value of correlation coefficient (r) for smeared method was higher than that of other method, indicating that a novel technique by smearing sCT powder on the surface of KBr pellet was the best optimal sample preparation method.

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Analysis of Polypeptide and Protein Structures Using Fourier Transform Infared Spectroscopy

Cited by 47 publications

References 29 publications

Infrared microspectroscopic imaging as a probing tool to fast distinguish chemical compositions in calcified deposits of prostatic calculi and calcific tendonitis

Infrared microspectroscopic imaging as a probing tool to fast distinguish chemical compositions in calcified deposits of prostatic calculi and calcific tendonitis

Kinetics of inclusion body formation studied in intact cells by FT‐IR spectroscopy

Different solid sample preparation methods affecting the spectral similarity of salmon calcitonin

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