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 awarded. themes similar to supramolecular constitution and association, thermodynamics and kinetics of meeting, in addition to the elemental mechanisms of protein-protein interactions are mentioned, and certain emphasis is given to utilized biophysical techniques.
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Additional resources for Cytoskeletal and Extracellular Proteins: Structure, Interactions and Assembly The 2nd International EBSA Symposium
Also Fraser & MacRae, 1982). g. , 1985). (ii) Contrasting of IF by low-angle shadowing accentuates an intrinsic axial repeat of about 22nm (Fig. , 1987). Several considerations imply that this repeat is specified by rod domain properties. , 1986). Moreover. the 22nm spacing correlates with the expected lengths of segments I and 2. , 1985). This proportionality is readily explained if IF of all kinds were to be made up of building-blocks that have modules of conserved length and mass (the rod domains) and modules of variable mass (the end-domains), and that IF are assembled by packing the conserved modules together in essentially the same way.
Aebi U, Cohn J. Buhle L. Gerace L (1986) The nuclear lamina is a meshwork of intermediatetype filaments. Nature(Lond) 323:560-564. Ahmadi B. Boston N M, Oobb M G, Speakman P T (1980) Possible four-chain repeating unit in the microfibril of wool. In: Parry 0 A 0 & Creamer L K (eds) Fibrous Proteins: Scientific. Industrial and Medical Aspects. vol 2. Academic Press. London. pp 161-166. Baker T S. Winkelmann 0 A (1986) Methodology for determining the three-dimensional structure of myosin S I from electron microscopy of orthogonal thin sections.
ImM DTT. 37°C). 0. (b) NF-L was dialyzed against filament reconstitution buffer. 5. (c) NF-L was dialyzed against standard filament reconstitution buffer. except at 20 o C. Temperature appears to be another crucial parameter to achieve correct NF-L assembly: Reconstitution of NF-L at 2()oC - under otherwise optimal reconstitution conditions (see above) results in short filamentous structures (Fig. 3c) which, after raising the temperature back to 37oC, can no longer form normal looking IF. Apparently, lowering the temperature significantly below 37°C leads to "dead-end" precursor structures that cannot be rescued by simply restoring the proper reconstitution temperature.