Two-Dimensional/Attenuated Total Reflection Infrared Correlation Spectroscopy Studies on Secondary Structural Changes in Human Serum Albumin in Aqueous Solutions: pH-Dependent Structural Changes in the Secondary Structures and in the Hydrogen Bondings of Side Chains

2001 ◽  
Vol 105 (20) ◽  
pp. 4763-4769 ◽  
Author(s):  
Koichi Murayama ◽  
Yuqing Wu ◽  
Bogusława Czarnik-Matusewicz ◽  
Yukihiro Ozaki
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Structural Changes ◽  
Total Reflection ◽  
Attenuated Total Reflection ◽  
Correlation Spectroscopy ◽  
Two Dimensional ◽  
Ph Dependent ◽  
Spectroscopy Studies ◽  
Hydrogen Bondings

Two-Dimensional Attenuated Total Reflection/Infrared Correlation Spectroscopy Studies on Concentration and Heat-Induced Structural Changes of Human Serum Albumin in Aqueous Solutions

2002 ◽  
Vol 56 (9) ◽  
pp. 1186-1193 ◽  
Author(s):  
Yuqing Wu ◽  
Koichi Murayama ◽  
Boguslawa Czarnik-Matusewicz ◽  
Yukihiro Ozaki
Keyword(s):  
Secondary Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Aqueous Solutions ◽  
Ir Spectra ◽  
Total Reflection ◽  
Attenuated Total Reflection ◽  
Correlation Spectroscopy ◽  
Random Coil ◽  
Two Dimensional

Attenuated total reflection (ATR)/FT-IR spectra were measured for human serum albumin (HSA) in aqueous solutions (pH 6.6) with concentrations of 1.0, 2.0, 3.0, 4.0, and 5.0 wt % over a temperature range of 45–80 °C. Generalized two-dimensional (2D) correlation spectroscopy was employed to explore concentration and heat-induced structural variations of HSA in aqueous solutions. To generate 2D correlation spectra, the raw spectra were subjected to the appropriate pretreatment procedure involving ATR correction, subtraction of the spectrum of an aqueous solution, and smoothing. The synchronous and asynchronous correlation spectra were calculated for the concentration-dependent IR spectral variations in the amide I region at various temperatures. The two-dimensional ATR/IR correlation spectra greatly enhance band separation in the region and provide information about the correlation between the amide bands of HSA arising from the same and different secondary structure components. Based on the correlation investigated and previously proposed relationship between the secondary structure elements and the amide band frequencies, we have proposed the detailed assignments in the amide I region at 45 and 80 °C. The proposed assignments are compared with those based on the results of second derivative and Fourier self-deconvolution (FSD) of the ATR/IR spectra. The asynchronous spectrum generated from the concentration-dependent spectral variations at 45 °C show that side chains, the random coil, and extended chains are more sensitive than the α-helices and β-turns to the concentration change. On the other hand, the corresponding spectrum at 80 °C reveals that the conformation changes in side chains and β-turns (or β-strands) of HSA start before those in extended chain, random coil structures, and α-helices.

scholarly journals Probing the secondary structure of bovine serum albumin during heat-induced denaturation using mid-infrared fiberoptic sensors

The Analyst ◽  
2015 ◽  
Vol 140 (3) ◽  
pp. 765-770 ◽  
Author(s):  
Rui Lu ◽  
Wen-Wei Li ◽  
Abraham Katzir ◽  
Yosef Raichlin ◽  
Han-Qing Yu ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Silver Halide ◽  
Total Reflection ◽  
Attenuated Total Reflection ◽  
Correlation Spectroscopy ◽  
Two Dimensional ◽  
Mid Infrared ◽  
First Time

Planar silver halide fiberoptic sensors were used for the first time for studying the mechanism of heating induced bovine serum albumin (BSA) denaturation by deconvoluted infrared attenuated total reflection (IR-ATR) spectra, and two-dimensional correlation spectroscopy (2D-CoS).

scholarly journals Two-dimensional infrared correlation spectroscopy studies on secondary structures and hydrogen bondings of side chains of proteins

2003 ◽  
Vol 17 (2-3) ◽  
pp. 79-100 ◽  
Author(s):  
Yukihiro Ozaki ◽  
Koichi Murayama ◽  
Yuqing Wu ◽  
Boguslawa Czarnik-Matusewicz
Keyword(s):  
Secondary Structures ◽  
Correlation Spectroscopy ◽  
Side Chains ◽  
Two Dimensional ◽  
2D Ir ◽  
Intensity Changes ◽  
Specific Order ◽  
Spectroscopy Studies ◽  
2D Correlation Spectroscopy ◽  
Hydrogen Bondings

This review paper reports usefulness of two-dimensional (2D) correlation spectroscopy in analyzing infrared (IR) spectra of proteins in aqueous solutions. In the 2D approach, spectral peaks are spread over the second dimension, thereby simplifying the visualization of complex spectra consisting of many overlapped bands, and enhancing spectral resolution. 2D correlation spectroscopy has a powerful deconvolution ability for highly overlapped amide I, amide II, and amide III bands of proteins, enabling these bands to be assigned to various secondary structures. It also provides the specific order of the spectral intensity changes taking place during the measurement on the value of controlling variable affecting the spectra. Therefore, one can monitor the order of secondary structure variations in proteins by using 2D IR correlation spectroscopy. 2D correlation spectroscopy also provides new insight into the hydrogen bondings of side chains of proteins. In this review the principles and advantages of 2D correlation spectroscopy are outlined first and then three examples of the applications of 2D IR spectroscopy to protein research are presented.

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