Further characterization of protein secondary structures in purple membrane by circular dichroism and polarized infrared spectroscopies.

Biophysical journal ·Vol. 48 ·No. 6 ·1985-12-00 ·Pages 873-6

Nabedryk E, Bardin AM, Breton J

Abstract

The conformation and the orientation of the protein secondary structures in purple membrane was analyzed by infrared absorption and linear dichroism of oriented membranes as well as by UV circular dichroism of bacteriorhodopsin in intact purple membrane and in lipid vesicles. A large amount (74 +/- 5%) of transmembrane alpha-helices is detected with no significant contribution of beta-sheet strands running perpendicular to the membrane plane. Thus, these data do not support the recent structural model proposed by Jap et al. (Biophys. J. 1983, 43:81-89).

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Nabedryk E

Bardin A M

Breton J

References (20)

20 references, click to expand

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Article Info

Journal

Biophysical journal

Abbr.

Biophys J

ISSN

0006-3495

DOI

10.1016/S0006-3495(85)83848-0

Published

1985-12-00

Pages

873-6

Language

English

Region

United States

NLM ID

0370626

PMCID

PMC1329418

External Links

PubMed source DOI: 10.1016/S0006-3495(85)83848-0 PMC Full Text View journal details

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Further characterization of protein secondary structures in purple membrane by circular dichroism and polarized infrared spectroscopies.

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