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Vibrational spectra and structure of myelin membranes (1987)

Ayala, G. ; Carmona, P. ; Cózar, M. ; [et al.]

Springer

European biophysics journal 14 (1987), S. 219-225

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ISSN: 1432-1017

Keywords: Myelin membrane ; non-denaturing detergents ; lipids ; proteolipid protein ; Raman and infrared spectra

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Physics

Notes: Abstract Raman and infrared spectroscopy have been simultaneously applied, for the first time, to the study of myelin membranes and their proteolipid protein (PLP) so as to obtain information on the secondary structure of proteins and the ordering of lipid chains. The vibrational spectra were recorded at physiological pH using a non-denaturing detergent (n-octyl-β-d-glucopyranoside) in phosphate buffer. Neither the buffer nor the detergent interfere spectroscopically with the amide bands from proteins. The spectra reveal that the predominant secondary structure in the polypeptide backbone in myelin is the helix. The proteolipid protein was found to be more disordered than the polypeptide arrangement of the myelin membrane, as deduced from the relative intensities and halfwidths of characteristic infrared amide I bands. β-form and turns are also present, the amount of these structures being higher in PLP. The study of the Raman spectra of vC-C and vC-H regions made it possible to obtain information on the lipid chain order.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00256355

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Conformational features of lipids and proteins in myelin membranes using Raman and infrared spectroscopy (1987)

Carmona, P. ; Ramos, J. M. ; De Cózar, M. ; [et al.]

Chichester [u.a.] : Wiley-Blackwell

Journal of Raman Spectroscopy 18 (1987), S. 473-476

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ISSN: 0377-0486

Keywords: Chemistry ; Analytical Chemistry and Spectroscopy

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Chemistry and Pharmacology , Physics

Notes: Myelin membrane and its proteolipid protein (PLP) have been examined by infrared and Raman spectroscopy to provide information about the secondary structure of proteins and conformation of lipid chains. Splitting of the amide I modes in the vibrational spectra and locations of amide A, I, II, III and V bands indicate that the polypeptide arrangement in both membrane systems is mainly helical. The β-form is also present, its amount being higher in PLP. Raman spectra in the C—C and C—H stretching regions show significant differences concerning intra- and inter-chain lipid order, which is greater in PLP.

Additional Material: 5 Ill.