منابع مشابه
Electrostatic colloid-membrane complexation
– We investigate numerically and on the scaling level the adsorption of a charged colloid on an oppositely charged flexible membrane. We show that the long ranged character of the electrostatic interaction leads to a wrapping reentrance of the complex as the salt concentration is varied. The membrane wrapping depends on the size of the colloid and on the salt concentration and only for intermed...
متن کاملElastic deformation of a fluid membrane upon colloid binding.
When a colloidal particle adheres to a fluid membrane, it induces elastic deformations in the membrane which oppose its own binding. The structural and energetic aspects of this balance are investigated within the framework of a Helfrich Hamiltonian. Based on the full nonlinear shape equations for the membrane profile, a line of continuous binding transitions and a second line of discontinuous ...
متن کاملPhotonic binding in silicon-colloid microcavities.
Photonic binding between two identical silicon-colloid-based microcavities is studied by using a generalized multipolar expansion. In contrast with previous works, we focus on low-order cavity modes that resemble low-energy electronic orbitals. For conservative light intensities, the interaction between cavity modes with moderate Q factors produces extremely large particle acceleration values. ...
متن کاملRetroviral matrix domains share electrostatic homology: models for membrane binding function throughout the viral life cycle.
The matrix domain (MA) of Gag polyproteins performs multiple functions throughout the retroviral life cycle. MA structures have an electropositive surface patch that is implicated in membrane association. Here, we use computational methods to demonstrate that electrostatic control of membrane binding is a central characteristic of all retroviruses. We are able to explain a wide range of experim...
متن کاملElectrostatic and Hydrophobic Interactions Differentially Tune Membrane Binding Kinetics of the C2 Domain of Protein
Background: The C2 domain is a Ca2 sensor that drives the first step in the activation of conventional PKC isozymes. Results:Hydrophobic interactions drive membrane association and electrostatic interactions drive membrane retention of the C2 domain. Conclusion: The amplitude and location of conventional PKC signaling is controlled by residues in the C2 domain. Significance: Point mutations in ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Europhysics Letters (EPL)
سال: 2004
ISSN: 0295-5075,1286-4854
DOI: 10.1209/epl/i2004-10068-x