Secondary Structure Determination by Means of ATR-FTIR Spectroscopy

2017 ◽  
pp. 195-203 ◽  
Author(s):  
Batoul Srour ◽  
Stefan Bruechert ◽  
Susana L. A. Andrade ◽  
Petra Hellwig
Keyword(s):  
Secondary Structure ◽  
Ftir Spectroscopy ◽  
Structure Determination

15N, 13C and 1H resonance assignments and secondary structure determination of a variable heavy domain of a heavy chain antibody

2013 ◽  
Vol 8 (1) ◽  
pp. 113-116 ◽  
Author(s):  
Christine E. Prosser ◽  
Lorna C. Waters ◽  
Frederick W. Muskett ◽  
Vaclav Veverka ◽  
Philip W. Addis ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Heavy Chain ◽  
Structure Determination ◽  
Resonance Assignments ◽  
Variable Heavy ◽  
Heavy Chain Antibody

Secondary structure determination for the Antennapedia homeodomain by nuclear magnetic resonance and evidence for a helix-turn-helix motif.

1988 ◽  
Vol 7 (13) ◽  
pp. 4305-4309 ◽  
Author(s):  
G. Otting ◽  
Y. Q. Qian ◽  
M. Müller ◽  
M. Affolter ◽  
W. Gehring ◽  
...  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Secondary Structure ◽  
Structure Determination ◽  
Nuclear Magnetic

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.

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