Coat proteins assembled state

Any polymerization reaction in which the product of each elongation step can itself also undergo further polymerization. When the same types of bonds and/or conformational states that are present in the reactant(s) are generated within product(s) during elongation, the process is referred to as isodesmic polymerization. Such is the case for the indefinite polymerization of actin, tubulin, hemoglobin S, and tobacco mosaic virus coat protein. See Nudeation Protein Polymerization Actin Assembly Kinetics Microtubule Assembly Kinetics Microtubule Assembly Kinetics... 

Figure 12 Diagram of assembled states of the coat protein of tobacco mosaic virus M free monomers, BD cylindrical disks, LW/H protohelices and helices. Symbols results from differential scanning microscopy DSC, titration, and sedimentation experiments, lines theory. The theory is based on binding energy Equation (9) and presumes competing repulsive Coulomb and attractive hydrophobic interactions (Kegel and van der Schoot, 2006).

After coat protein pen tamer formation, the < (>X174 internal scaffolding protein binds to the underside of the pentamer and induces a conformational change in the particle. This change inhibits premature aggregation, and produces an assembly-competent state. B-protein binding is both necessary and sufficient to allow future interactions with... 

The S-layer protein SbsB reassembles into flat mono- and double-layer sheets with a size of 1-3 p.m [80]. The addition of the purified high molecular weight secondary cell wall polymer which functions as an anchoring structure for the S-layer protein in the bacterial cell wall [81] inhibited the in vitro self-assembly of the isolated S-layer protein and kept it in the water-soluble state. Interestingly, the soluble monomeric and/or oligomeric S-layer protein recrystallized into closed monolayers on poly-L-lysine coated EM-grids to which the S-... 

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