New Fourier transform infrared based computational method for peptide secondary structure determination. I. Description of method

Biopolymers ◽  
2001 ◽  
Vol 62 (2) ◽  
pp. 95-108 ◽  
Author(s):  
Mario Simonetti ◽  
Carlo Di Bello
Keyword(s):  
Fourier Transform ◽  
Secondary Structure ◽  
Structure Determination ◽  
Fourier Transform Infrared ◽  
Computational Method ◽  
Peptide Secondary Structure

Secondary structure in properdin of the complement cascade and related proteins: a study by Fourier transform infrared spectroscopy

Biochemistry ◽  
1989 ◽  
Vol 28 (18) ◽  
pp. 7176-7182 ◽  
Author(s):  
Stephen J. Perkins ◽  
Adam S. Nealis ◽  
Parvez I. Haris ◽  
Dennis Chapman ◽  
Dimitrios Goundis ◽  
...  
Keyword(s):  
Fourier Transform ◽  
Infrared Spectroscopy ◽  
Secondary Structure ◽  
Fourier Transform Infrared Spectroscopy ◽  
Fourier Transform Infrared ◽  
Complement Cascade ◽  
Related Proteins

Fourier-Transform Infrared Spectroscopic Investigation of the Secondary Structure of P2 Protein in Deuterium Oxide Solution

1991 ◽  
Vol 44 (11) ◽  
pp. 1523 ◽  
Author(s):  
BH Stuart ◽  
EF Mcfarlane
Keyword(s):  
Fourier Transform ◽  
Secondary Structure ◽  
Deuterium Oxide ◽  
Resolution Enhancement ◽  
Low Frequency ◽  
Fourier Transform Infrared ◽  
Crystallographic Study ◽  
Fitting Procedures ◽  
P2 Protein ◽  
Α Helix

Fourier transform infrared ( F.t.i.r .) spectroscopy has been used to investigate the secondary structure of bovine P2 protein in deuterium oxide (D2O) solution. The amide 1 region of the spectrum was analysed quantitatively by means of resolution enhancement and band-fitting procedures. The protein was found to consist mainly of β-structure (61%), with a small amount of α-helix (11%). A reason for the existence of an unusually intense low-frequency band assigned to β-structure is discussed. The F.t.i.r . results are compared with those from an X-ray crystallographic study and from circular dichroism and explanations are offered for discrepancies between the results from the different methods.

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.

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