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 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.

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.

scholarly journals Effect of oxidative treatment on the secondary structure of decoloured bloodmeal

RSC Advances ◽  
2014 ◽  
Vol 4 (59) ◽  
pp. 31201-31209 ◽  
Author(s):  
Talia Hicks ◽  
Casparus J. R. Verbeek ◽  
Mark C. Lay ◽  
James M. Bier
Keyword(s):  
Fourier Transform ◽  
Spatial Distribution ◽  
Secondary Structure ◽  
Ftir Spectroscopy ◽  
Peracetic Acid ◽  
Fourier Transform Infrared ◽  
Secondary Structures ◽  
Oxidative Treatment

Synchrotron-based Fourier-transform infrared (FTIR) spectroscopy was used to assess the effect of peracetic acid decolouring on the spatial distribution of secondary structures within particles of bloodmeal.

Secondary structure analysis of purified functional CHIP28 water channels by CD and FTIR spectroscopy

Biochemistry ◽  
1993 ◽  
Vol 32 (44) ◽  
pp. 11847-11856 ◽  
Author(s):  
Alfred N. van Hoek ◽  
Michael Wiener ◽  
S. Bicknese ◽  
Larry Miercke ◽  
Joachim Biwersi ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Ftir Spectroscopy ◽  
Structure Analysis ◽  
Water Channels ◽  
Secondary Structure Analysis

Secondary Structure of Monoamine Oxidase by FTIR Spectroscopy

1995 ◽  
Vol 208 (2) ◽  
pp. 773-778 ◽  
Author(s):  
J. Wouters ◽  
R. Ramsay ◽  
E. Goormaghtigh ◽  
J.M. Ruysschaert ◽  
R. Brasseur ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Monoamine Oxidase ◽  
Ftir Spectroscopy

Secondary Structure and Orientation of Phospholamban Reconstituted in Supported Bilayers from Polarized Attenuated Total Reflection FTIR Spectroscopy

Biochemistry ◽  
1995 ◽  
Vol 34 (13) ◽  
pp. 4448-4456 ◽  
Author(s):  
Suren A. Tatulian ◽  
Larry R. Jones ◽  
Laxma G. Reddy ◽  
David L. Stokes ◽  
Lukas K. Tamm
Keyword(s):  
Secondary Structure ◽  
Ftir Spectroscopy ◽  
Total Reflection ◽  
Attenuated Total Reflection ◽  
Supported Bilayers
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