New Fourier transform infrared based computational method for peptide secondary structure determination. II. Application to study of peptide fragments reproducing processing site of ocytocin-neurophysin precursor

Biopolymers ◽  
2001 ◽  
Vol 62 (2) ◽  
pp. 109-121 ◽  
Author(s):  
Mario Simonetti ◽  
Carlo Di Bello
Biochemistry ◽  
1989 ◽  
Vol 28 (18) ◽  
pp. 7176-7182 ◽  
Author(s):  
Stephen J. Perkins ◽  
Adam S. Nealis ◽  
Parvez I. Haris ◽  
Dennis Chapman ◽  
Dimitrios Goundis ◽  
...  

1991 ◽  
Vol 44 (11) ◽  
pp. 1523 ◽  
Author(s):  
BH Stuart ◽  
EF Mcfarlane

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.


RSC Advances ◽  
2014 ◽  
Vol 4 (59) ◽  
pp. 31201-31209 ◽  
Author(s):  
Talia Hicks ◽  
Casparus J. R. Verbeek ◽  
Mark C. Lay ◽  
James M. Bier

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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