Pressure-induced secondary structure changes of ribonuclease A and ribonuclease S studied by FTIR spectroscopy

1995 ◽  
Vol 1 (3) ◽  
pp. 207-216 ◽  
Author(s):  
Naohiro Takeda ◽  
Minoru Kato ◽  
Yoshihiro Taniguchi
Keyword(s):  
Secondary Structure ◽  
Ftir Spectroscopy ◽  
Ribonuclease A ◽  
Structure Changes

scholarly journals Systematic FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin under Various Denaturation Conditions

Biomolecules ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 359 ◽  
Author(s):  
Usoltsev ◽  
Sitnikova ◽  
Kajava ◽  
Uspenskaya
Keyword(s):  
Secondary Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Ftir Spectroscopy ◽  
Conformational Changes ◽  
Data Interpretation ◽  
Random Coil ◽  
Helical Conformation ◽  
Structure Changes

Human serum albumin (HSA) is the most abundant protein in blood plasma. HSA is involved in the transport of hormones, fatty acids, and some other compounds, maintenance of blood pH, osmotic pressure, and many other functions. Although this protein is well studied, data about its conformational changes upon different denaturation factors are fragmentary and sometimes contradictory. This is especially true for FTIR spectroscopy data interpretation. Here, the effect of various denaturing agents on the structural state of HSA by using FTIR spectroscopy in the aqueous solutions was systematically studied. Our data suggest that the second derivative deconvolution method provides the most consistent interpretation of the obtained IR spectra. The secondary structure changes of HSA were studied depending on the concentration of the denaturing agent during acid, alkaline, and thermal denaturation. In general, the denaturation of HSA in different conditions is accompanied by a decrease in α-helical conformation and an increase in random coil conformation and the intermolecular β-strands. Meantime, some variation in the conformational changes depending on the type of the denaturation agent were also observed. The increase of β-structural conformation suggests that HSA may form amyloid-like aggregates upon the denaturation.

Using synchrotron FTIR spectroscopy to determine secondary structure changes and distribution in thermoplastic protein

2013 ◽  
Vol 130 (1) ◽  
pp. 359-369 ◽  
Author(s):  
James Michael Bier ◽  
Casparus Johannes Reinhard Verbeek ◽  
Mark Christopher Lay
Keyword(s):  
Secondary Structure ◽  
Ftir Spectroscopy ◽  
Structure Changes ◽  
Thermoplastic Protein

scholarly journals On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy

Molecules ◽  
2021 ◽  
Vol 26 (4) ◽  
pp. 970
Author(s):  
Jelica Milošević ◽  
Radivoje Prodanović ◽  
Natalija Polović
Keyword(s):  
Secondary Structure ◽  
Ftir Spectroscopy ◽  
Internal Standard ◽  
Thioflavin T ◽  
Lag Phase ◽  
Standard Methods ◽  
Qualitative And Quantitative ◽  
Structure Changes ◽  
Tht Fluorescence ◽  
Amyloid Fibrillation

Oligomeric intermediates on the pathway of amyloid fibrillation are suspected as the main cytotoxins responsible for amyloid-related pathogenicity. As they appear to be a part of the lag phase of amyloid fibrillation when analyzed using standard methods such as Thioflavin T (ThT) fluorescence, a more sensitive method is needed for their detection. Here we apply Fourier transform infrared spectroscopy (FTIR) in attenuated total reflectance (ATR) mode for fast and cheap analysis of destabilized hen-egg-white lysozyme solution and detection of oligomer intermediates of amyloid fibrillation. Standard methods of protein aggregation analysis— Thioflavin T (ThT) fluorescence, atomic force microscopy (AFM), and 8-anilinonaphthalene-1-sulphonic acid (ANS) fluorescence were applied and compared to FTIR spectroscopy data. Results show the great potential of FTIR for both, qualitative and quantitative monitoring of oligomer formation based on the secondary structure changes. While oligomer intermediates do not induce significant changes in ThT fluorescence, their secondary structure changes were very prominent. Normalization of specific Amide I region peak intensities by using Amide II peak intensity as an internal standard provides an opportunity to use FTIR spectroscopy for both qualitative and quantitative analysis of biological samples and detection of potentially toxic oligomers, as well as for screening of efficiency of fibrillation procedures.

The Secondary Structure of the Inhibited Mitochondrial ADP/ATP Transporter from Yeast Analyzed by FTIR Spectroscopy†

Biochemistry ◽  
2001 ◽  
Vol 40 (30) ◽  
pp. 8821-8833 ◽  
Author(s):  
Víctor A. Lórenz ◽  
Joaquim Villaverde ◽  
Véronique Trézéguet ◽  
Guy J.-M. Lauquin ◽  
Gérard Brandolin ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Ftir Spectroscopy

scholarly journals Electromagnetic Fields Effects on the Secondary Structure of Lysozyme and Bioprotective Effectiveness of Trehalose

2012 ◽  
Vol 2012 ◽  
pp. 1-6 ◽  
Author(s):  
Emanuele Calabrò ◽  
Salvatore Magazù
Keyword(s):  
Electromagnetic Field ◽  
Spectral Analysis ◽  
Secondary Structure ◽  
Mobile Phone ◽  
Ftir Spectroscopy ◽  
Electromagnetic Fields ◽  
Low Frequency ◽  
Ftir Spectra ◽  
Vibration Band ◽  
Extremely Low Frequency

FTIR spectroscopy was used to investigate the effects of extremely low frequency (50 Hz) electromagnetic field and of microwaves at 900 MHz on the secondary structure of a typical protein, the lysozyme, evaluating the bioprotective effectiveness of trehalose. Lysozyme in D2O solution (60 mg/ml) was exposed to 50 Hz frequency electromagnetic field at 180 μT. The FTIR spectra indicated an increase of CH2 group at 1921 and 1853 cm−1 after 3 h of exposure. Such effect was not observed after the addition of trehalose (150 mg/mL) at the same exposure conditions. Lysozyme dissolved in D2O at the concentration of 100 mg/mL was exposed up to 4 h to 900 MHz mobile phone microwaves at 25 mA/m. A significant increase in intensity of the amide I vibration band in the secondary structure of the protein was observed after 4 h exposure to microwaves. This effect was inhibited by the presence of trehalose at the concentration of 150 mg/mL. Fourier self-deconvolution spectral analysis of lysozyme in D2O solution after exposure to microwaves revealed an increase in intensity of the conformational components of amide I mode, particularly of β-sheet and turn that can be attributed to disorder and unfolding processes of the protein.

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