Fourier Transform Infrared Spectrometric Analysis of Protein Conformation: Effect of Sampling Method and Stress Factors

Weert, Marco van de; Haris, Parvez I.; Hennink, Wim E.; Crommelin, Daan J.A.

doi:10.1006/abio.2001.5337

Cited by 228 publications

(163 citation statements)

References 42 publications

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“…Marco, V. D. W. et al [36] have studied protein conformation with the help of this technique. They have reported that changes in the amide bands in Fourier transform infrared spectra of proteins are attributed to alterations in protein secondary structure.…”

Section: Review Of the Literaturementioning

confidence: 99%

Vibrational Studies of Different Human Body Disorders Using FTIR Spectroscopy

Kumar¹,

Reena²,

Chaudhary³

et al. 2014

OJAppS

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Some of the important features of the bands occur in the present study. The band called amide A is available in all the diseased and healthy controls and the frequency of the band ranges from 3380 cm −1 to 3480.74 cm −1 . The band due to C-H band and called hydrocarbon band was found only in paralytic and Alzheimer diseased along with normal healthy controls. Carbide band (C=C) is found only in Duchenne muscular dystrophy, paralytic and Alzheimer's disease patients. Amide I was intact in all disorders with normal persons. Peroxide band (O-O) was found in all the cases of study. Amide IV band was found in paralytic, muscular dystrophy, Alzheimer's diseases and normal controls. The amide V band was found in Alzheimer's diseases only. The appearance or disappearance of the bands is a good sign to understand the mechanisms at the molecular level. FTIR spectroscopy may help in the diagnosis of the disease at the early stage of the onset. This spectroscopy can be used nicely for the study of hair, vaginal fluid, nails, urine, mucus, semen, synovial fluid, blood, hemoproteins, skin, and tears for human beings. We can also use it to understand the effect of adulteration on food and paint technology. FTIR is an indicator to explore the changes occurring at molecular level.

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Section: Review Of the Literaturementioning

confidence: 99%

Vibrational Studies of Different Human Body Disorders Using FTIR Spectroscopy

Kumar¹,

Reena²,

Chaudhary³

et al. 2014

OJAppS

View full text Add to dashboard Cite

show abstract

“…Whenever necessary, residual contributions due to atmospheric water vapor and CO 2 were eliminated by subtraction of the corresponding spectra from the registered samples' spectra, in order to obtain a flat baseline between 2300 and 1850 cm À1 [29]. The resultant protein spectra were smoothed with a seven-point (13 cm…”

Section: Data Analysis Of Ftir Spectramentioning

confidence: 99%

Characterization of S-layer proteins of Lactobacillus by FTIR spectroscopy and differential scanning calorimetry

Mobili

Londero

Maria

et al. 2009

Vibrational Spectroscopy

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“…There are several experimental methods available for determination of protein secondary structure, such as circular dichroism (CD) (Shanmugam & Polavarapu, 2006), nuclear magnetic resonance (NMR) , X-ray scattering and diffraction , calorimetry and fluorescence (Gelamo et al, 2002), diffuse reflectance (DR) (Ishida & Griffiths, 1993), electron paramagnetic resonance ESR (Gelamo et al, 2004), Raman (Bolton & Scherer, 1989), near infrared (NIR) (Wu et al, 2000) and IR spectroscopy (Cai & Singh, 1999;Grdadolnik & Maréchal, 2001a& 2001bJackson et al, 1989;Maréchal, 2004Maréchal, & 2003van de Weert et al, 2001;Zhang & Yan, 2005). The last has for many years been a promising technique for the determination of the secondary structure of proteins in that some peptide vibrations are sensitive to conformation (Harris & Chapman, 1992;Jackson & Mantsch, 1995).…”

Section: Proteinsmentioning

confidence: 99%