Independent nucleation

This enzyme from E. coli is a tetramer of four identical subunits, each of molecular weight 116,500. Amber and ochre (premature termination) mutants of the enzyme provide a number of enzymically inactive, incomplete peptide chains, identical in sequence with the N-term nal part of the wild-type chains. A subset of these N-terminal peptides, called acceptor peptides, can combine with so-called wild-type chain, to restore enzymic activity (Ullmann et al., 1965, 1967 Ullmann and Perrin, 1970 see also the review by Zabin and Villarejo, 1975). Goldberg (1969) suggested that the acceptor peptides and the [Pg.63]

Independently Nucleated Units of Structure (LINUS) breaks the problem down by first identifying local regions likely to have a particular secondary structure and then folds them together to minimize the energy. 

According to the theory of the metastable adsorption of de Gennes [172], when an adsorbed polymer layer is in contact with a pure solvent, the layer density diminishes from the substrate (e.g., metal) surface. The behavior of several polymer film electrodes (e.g., poly(tetra-cyanoquinodimethane) [173], poly(vinyl-ferrocene) [21, 92], polypyrrole [174], and polyaniline [37, 175]) has been explained by the assumption that the film density decreases with the film thickness, that is from the metal surface to the polymer/solution interface. During electropolymerization (e.g., in the case of polyaniline) first, a compact layer (thickness L 200 nm) is formed on the electrode surface via a potential-independent nucleation and a... 

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