Secondary structure of the hydrophobic myelin protein in a lipid environment as determined by Fourier-transform infrared spectrometry

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TypeArticle
Journal titleThe Journal of Biological Chemistry
ISSN1083-351X
Volume262
Issue18
Pages85988602
AbstractThe secondary structure of a hydrophobic myelin protein (lipophilin), reconstituted with dimyristoylphosphatidylcholine or dimyristoylphosphatidylglycerol, was investigated by Fourier-transform infrared spectroscopy. Protein infrared spectra in the amide I region were analyzed quantitatively using resolution enhancement and band fitting procedures. Lipophilin in a phospholipid environment adopts a highly ordered secondary structure which at room temperature consists predominantly of alpha-helix (approximately 55%) and beta-type conformations (36%). The secondary structure of the protein is not affected by the lipid gel to liquid crystalline phase transition. Heating of the lipid-protein complex above approximately 35 degrees C results in a gradual decrease in alpha-helical content, accompanied by an increase in the amount of beta-structures. Lipophilin dissolved in 2-chloroethanol is, compared to the protein in a lipid environment, richer in the alpha-helical conformation but still contains a sizable amount of beta-structure.
Publication date
PublisherThe American Society for Biochemistry and Molecular Biology, Inc.
Linkhttp://www.jbc.org/content/262/18/8598.abstract
LanguageEnglish
AffiliationNational Research Council Canada
Peer reviewedYes
NPARC number23001359
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Record identifier1e3a0e6a-91f3-49dc-976c-215d3e23fba9
Record created2017-01-23
Record modified2017-01-23
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