By Daniel M. Bollag, Michael D. Rozycki, Stuart J. Edelstein (auth.), Professor Dr. Ueli Aebi, Professor Dr. Jürgen Engel (eds.)
In this quantity the contributions of the second overseas EBSA (European Biophysical Societies organization) Symposium dedicated to the biophysical and biochemical elements of the constitution and interplay of cytoskeletal and extracellular proteins are provided. subject matters reminiscent of supramolecular constitution and association, thermodynamics and kinetics of meeting, in addition to the fundamental mechanisms of protein-protein interactions are mentioned, and specific emphasis is given to utilized biophysical techniques.
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Extra resources for Cytoskeletal and Extracellular Proteins: Structure, Interactions and Assembly The 2nd International EBSA Symposium
Example text
On the contrary, our data demonstrate that native NF are the most polymorphic filaments that we have examined, and that 38 Fig. 4: MPL histograms measured from native NF (a), 6-M-urea solubilized/reconstituted NF (b), and reconstituted NF-L (c) filaments by scanning transmission electron microscopy (STEM). , 1985]. g. the NF-L filaments - exhibit minimal MPL-polymorphism. Clearly, more work needs to be done for understanding the cause and ultimate significance of the IF MPL-polymorphism. Acknowledgements We would like to thank Dr.
And a research award from the Maurice E. A. ). E. Fowler, P. -T. Sun (1983). The Fibrillar Substructure of Keratin Filaments Unraveled. J. Cell Bioi. 97: 1131-1143. , M. C. Troncoso, R. Eichner, and A. Engel (1988). Unifying Principles in Intermediate Filament (IF) Structure and Assembly. Protoplasma 145: 73-81. , G. Filliatreau, F. Boutteau, G. Biserte, and J. Schrevel (1980). Study of the lO-nm Filament Fraction During the Standard Microtubule Preparation. Biochem. J. 191: 543-546. , R. Eichner, and U.
Whereas both IF end-domains are often of comparable size. the myosin end-domains are lop-sided, the aminoterminal end-domain being vestigial whereas thc carboxy-terminal end-domain, subfragment I (SI) is very large, - IOOkDa. This is the domain to which the myosin light chains bind, and where the ATPase activity essential to force generation resides. In the myosin filament, the respective functions of the rod domain and of the end-domain are well understood. The rod domains are polymerized into a stable inextensible filament backbone, and the S I-crossbridges extend from this matrix to couple cyclically with another cytoskeletal element, the actin filament.