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A fourier transform infrared spectroscopic study of P2 protein in reconstituted myelin
Author(s) -
Stuart B. H.
Publication year - 1996
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549600201691
Subject(s) - fourier transform infrared spectroscopy , protein secondary structure , myelin , aqueous solution , chemistry , infrared spectroscopy , fourier transform , biophysics , protein structure , helix (gastropod) , infrared , crystallography , biochemistry , biology , central nervous system , organic chemistry , chemical engineering , mathematical analysis , ecology , physics , mathematics , optics , snail , engineering , neuroscience
The secondary structure of P2 protein, isolated from bovine peripheral nervous system myelin, in reconstituted myelin was studied using Fourier transform infrared (FTIR) spectroscopy. Spectra of the protein in aqueous solution and in the lipid environment were compared and notable changes were observed. It was proposed that there are significant differences in the conformation of the protein in the contrasting environments. An increase in α‐helical structure was observed for the protein in myelin and the significant amount of β‐structure observed in aqueous solution was reduced. The degree of α‐helix appears to be related to the neuritogenic activity of the P2 protein. The findings of this study also support the view that the presence of both α‐helices and β‐structure plays a significant role in membrane proteins.