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Dynamic aspects of the incorporation of proteins into biological membranes
Author(s) -
Horváth L. I.,
Török M.,
Hideg K.,
Dux L
Publication year - 1997
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/(sici)1099-1352(199707/08)10:4<188::aid-jmr364>3.0.co;2-p
Subject(s) - chemistry , rotational diffusion , viscosity , membrane , transmembrane protein , membrane protein , aqueous solution , chemical physics , biophysics , materials science , biochemistry , organic chemistry , molecule , receptor , composite material , biology
The contributions of intramembranous and extramembranous segments of transmembrane proteins to frictional forces have been studied by covalently attached 14 N‐ and 15 N‐indane dione and maleimide spin labels using saturation transfer electron spin resonance spectroscopy. The role of molecular size and membrane viscosity is discussed in determining rotational mobilities of proteins. By comparing the measured rotational correlation times with the predictions of hydrodynamic models the aggregation states of transmembrane proteins is estimated. On increasing the viscosity of the aqueous phase by polyols the viscous drag of the extramembranous segments of proteins is increased and from systematic hydrodynamic measurements the size of the protruding segments can be estimated. The role of slowed molecular diffusion is briefly discussed in the inhibition of enzymatic activity. © 1997 John Wiley & Sons, Ltd.