Robert borgon vinculin thesis …

α-Actinin is a rod-shaped antiparallel dimer of two 100-kDa monomers; this configuration positions its actin-binding CH motifs at either end of the rigid rod, an arrangement that allows α-actinin to efficiently cross-link actin filaments into tight bundles (, ). The central rod domain of α-actinin contains four spectrin repeats (R1 to R4), which are triple-helical coiled-coil bundles that are connected by helical linkers (, ). In α-actinin, these repeats are aligned in a symmetric fashion that allows for the formation of the rigid dimer through interactions of the R1 and R4 repeats and of the R2 and R3 repeats (, ). However, spectrin repeats can also form stable unfolded intermediates when subjected to mechanical stress (), as occurs following the formation of adhesion complexes, and the spectrin repeats of α-actinin also harbor docking sites for a number of other cytoskeletal proteins (), in particular vinculin ().

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Note: Published in Molecular and Cellular Biology ; Philippe R. J. Bois, Robert A. Borgon, Clemens Vonrhein, and Tina Izard; "Structural Dynamics of -Actinin-Vinculin Interactions"

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Robert Borgon Vinculin Thesis
Robert Borgon ii ABSTRACT The HIV pandemic has affected millions of people around the world both medically and socially, since there is a stigma associated with this disease

Structure of the α-Actinin–Vinculin Head Domain …

αVBS binding provokes dramatic conformational changes in Vh1 that displace Vt, which in the context of full-length vinculin would be predicted to release its five domains and allow vinculin to be free to interact with other binding partners. Thus, collectively, these findings suggest a domino effect of structural alterations in adhesion signaling, whereby alterations in the structure of one protein (α-actinin) might then provoke changes in the structure and function of another (vinculin), in effect a chain reaction of structural signals.

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2012/04/06 · National Academy of Sciences ..

The protease cleavage patterns of talin-VBS1- and talin-VBS3-bound vinculin were essentially equivalent (Fig. , top left), in agreement with their nearly identical effects on the structure of the Vh1 domain (, ). However, obvious differences were evident in talin- versus α-actinin-bound vinculin when the peptide fragments of talin-VBS1- or talin-VBS3-bound vinculin were compared to those generated in αVBS-bound vinculin. Specifically, Ala-490, which resides in the loop between the Vh2 and Vh3 domains, was much more susceptible to cleavage in talin-VBS3-bound vinculin than in αVBS-bound vinculin (Fig. , middle). In inactive vinculin, Ala-490 resides at the interface of the Vh2-Vt interdomain interaction (), and thus displacement of Vt by the binding of talin's VBSs to the Vh1 domain must also disrupt the Vh2-Vt interface, but this does not occur to a significant extent in αVBS-bound vinculin. Therefore, the unique structural alterations in the Vh1 domain caused by the binding of talin's VBSs versus αVBS (Fig. ) appear to also cause unique conformational changes in far-distant regions of the entire molecule.

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The images show how a protein called alpha-actinin partly unravels its structure to free an internal molecular "arm" that reaches out to another protein, called vinculin. This triggers vinculin to partly unravel as well, freeing several molecular "fingers" that assume a shape that allows alpha-actinin to bind to its partner.