Possible role of the highly conserved amino acids Trp-8 and Pro-13 in the N-terminal segment of the pigment-binding poly eptide LHI α of Rhodobacter capsulatus

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Abstract

Trp-8 and Pro-13 of the Rhodobacter capsulatus light-harvesting (LH) I α polypeptide are highly conserved among LHI and LHII α proteins of several species of the Rhodospirillaceae. Exchange of Trp-8 and Pro-13 to other amino acyl residues similar in structure and/or hydrophobicity indicates that Trp-8 is involved in the insertion of the LHI α polypeptide into the intracytoplasmic membrane (ICM). Pro-13, however, seems not to participate in the integration process of the LHI α protein but seems to be important for stable insertion of the LHI β partner protein in the ICM. © 1991.

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Richter, P., Cortez, N., & Drews, G. (1991). Possible role of the highly conserved amino acids Trp-8 and Pro-13 in the N-terminal segment of the pigment-binding poly eptide LHI α of Rhodobacter capsulatus. FEBS Letters, 285(1), 80–84. https://doi.org/10.1016/0014-5793(91)80729-M

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