Titlebook: Cytoskeletal and Extracellular Proteins; Structure, Interacti Ueli Aebi,Jürgen Engel Conference proceedings 1989 Springer-Verlag Berlin Hei

BARGE

incredulity

0932-2353 structure and organization, thermodynamics and kinetics of assembly, as well as the basic mechanisms of protein-protein interactions are discussed, and special emphasis is given to applied biophysical techniques.978-3-642-73927-9978-3-642-73925-5Series ISSN 0932-2353 Series E-ISSN 1868-2561

spondylosis

Conference proceedings 1989iochemical aspects of the structure and interaction of cytoskeletal and extracellular proteins are presented. Topics such as supramolecular structure and organization, thermodynamics and kinetics of assembly, as well as the basic mechanisms of protein-protein interactions are discussed, and special

隼鹰

虚弱

Christian Bär,Jens Fiege,Markus Weißysical and molecular biological experiments concerning both static and dynamic properties of IF proteins; to examine how far their resemblance to myosin extends; and to explore its implications for the functions - still rather vaguely defined - that are exercised by IF in cells.

SUGAR

,Risiken der Künstlichen Intelligenz,ration (Holmes, et al. 1989). The best of the five possible solutions resulting from the low resolution search is shown in Fig. 2. The (intensity) R-factor is 0.12. To refine at high resolution we adopted an iterative least squares procedure. However, no solution would refine satisfactorily. The resulting R-factors ranged from 0.37–0.45.

hieroglyphic

可憎

枯萎将要

The Structure of F-Actin Calculated from X-Ray Fibre Diagrams and the 0.6 nm Crystal Structureration (Holmes, et al. 1989). The best of the five possible solutions resulting from the low resolution search is shown in Fig. 2. The (intensity) R-factor is 0.12. To refine at high resolution we adopted an iterative least squares procedure. However, no solution would refine satisfactorily. The resulting R-factors ranged from 0.37–0.45.

委派

Christian Bär,Jens Fiege,Markus Weißer known paracrystals, the repeats of tau vary over a wide range (from 22 nm to 68 nm) while retaining the relative positions of their protein domains. This suggests that tau has unusual elastic properties.