NDLI: Structure-activity relationship in vinculin: an IR/attenuated total reflection spectroscopic and film balance study.

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Structure-activity relationship in vinculin: an IR/attenuated total reflection spectroscopic and film balance study.

Content Provider	Semantic Scholar
Author	Fringeli, Urs Peter Leutert, P. Thurnhofer, H. Fringeli, M. Burger, Max M.
Copyright Year	1986
Abstract	Surfacing and membrane-penetrating ability of vinculin and bovine serum albumin have been studied on a macroscopic level by means of a Langmuir film balance and on a molecular level by means of infrared attenuated total reflection spectroscopy. It is suggested that the driving force of the nonspontaneous process of membrane penetration by native vinculin is the spontaneous formation of rigid vinculin monolayers in the membrane. Lateral adhesion of vinculin molecules results from the formation of intermolecular pleated-sheet structures. Vinculin surface activity was found to result from an alpha-helical segment oriented approximately perpendicular to plane of the membrane. There is a conformational equilibrium between this helix and random structure. High ionic strength (110 mM) favors helix formation that leads to the greater than 100-fold enhancement of surfacing velocity relative to the velocity observed at a lower ionic strength (10 mM). Vinculin has a second helical segment oriented parallel to the plane of the membrane that is in a conformational equilibrium with the pleated-sheet structure.
File Format	PDF HTM / HTML
DOI	10.1073/pnas.83.5.1315
PubMed reference number	3081894
Journal	Medline
Volume Number	83
Issue Number	5
Alternate Webpage(s)	http://www.pnas.org/content/83/5/1315.full.pdf
Alternate Webpage(s)	https://doi.org/10.1073/pnas.83.5.1315
Journal	Proceedings of the National Academy of Sciences of the United States of America
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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