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Probing origins of molecular interactions stabilizing the membrane proteins halorhodopsin and bacteriorhodopsin
BIOTEC, University of Technology, 01307 Dresden, Germany..ORCID iD: 0000-0001-9919-0075
2005 (English)In: Structure, ISSN 0969-2126, E-ISSN 1878-4186, Vol. 13, no 2, p. 235-242Article in journal (Refereed) Published
Abstract [en]

Single-molecule atomic force microscopy and spectroscopy were applied to detect molecular interactions stabilizing the structure of halorhodopsin (HR), a light-driven chloride pump from Halobacterium salinarum. Because of the high structural and sequence similarities between HR and bacteriorhodopsin, we compared their unfolding pathways and polypeptide regions that established structurally stable segments against unfolding. Unfolding pathways and structural segments stabilizing the proteins both exhibited a remarkably high similarity. This suggests that different amino acid compositions can establish structurally indistinguishable energetic barriers. These stabilizing domains rather result from comprehensive interactions of all amino acids within a structural region than from specific interactions. However, one additional unfolding barrier located within a short segment of helix E was detected for HR. This barrier correlated with a Pi-bulk interaction, which locally disrupts helix E and divides a structural stabilizing segment.

Place, publisher, year, edition, pages
2005. Vol. 13, no 2, p. 235-242
National Category
Structural Biology
Identifiers
URN: urn:nbn:se:umu:diva-156784DOI: 10.1016/j.str.2004.12.005PubMedID: 15698567OAI: oai:DiVA.org:umu-156784DiVA, id: diva2:1292014
Available from: 2019-02-26 Created: 2019-02-26 Last updated: 2019-03-07Bibliographically approved

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Cisneros, David A.

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