Theoretical comparison of the self diffusion and mutual diffusion of interacting membrane proteins.
AUTOR(ES)
Scalettar, B A
RESUMO
Self diffusion and mutual diffusion in two-dimensional membrane systems are analyzed. It is shown that interprotein interactions can produce markedly different density-dependent changes in the diffusion coefficients describing these two processes; the qualitative differences are illustrated by using a theoretical formalism valid for dilute solutions. Results are obtained for three analytical potentials: hard-core repulsions, soft repulsions, and soft repulsions with weak attractions. Self diffusion is inhibited by all three interactions. In contrast, mutual diffusion is inhibited by attractions but is enhanced by repulsions. It is shown that such interaction-dependent differences in self diffusion and mutual diffusion could underlie, among other things, the disparity in protein diffusion coefficients extracted from fluorescence recovery after photobleaching and postelectrophoresis relaxation data.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=282050Documentos Relacionados
- Strategies for the identification of interacting proteins.
- Structural comparison of Neisseria gonorrhoeae outer membrane proteins.
- Dissolution of erythrocyte membranes in water and comparison of the membrane protein with other structural proteins.
- Self-degradation of heat shock proteins.
- A proposed mechanism for the self-splicing of proteins.