2,788 research outputs found
Universality classes in folding times of proteins
Molecular dynamics simulations in simplified models allow one to study the
scaling properties of folding times for many proteins together under a
controlled setting. We consider three variants of the Go models with different
contact potentials and demonstrate scaling described by power laws and no
correlation with the relative contact order parameter. We demonstrate existence
of at least three kinetic universality classes which are correlated with the
types of structure: the alpha-, alpha--beta-, and beta- proteins have the
scaling exponents of about 1.7, 2.5, and 3.2 respectively. The three classes
merge into one when the contact range is truncated at a 'reasonable' value. We
elucidate the role of the potential associated with the chirality of a protein.Comment: 22 pages, 21 figures, to appear in Biophys
Protein folding and models of dynamics on the lattice
We study folding in 16-monomer heteropolymers on the square lattice. For a
given sequence, thermodynamic properties and stability of the native state are
unique. However, the kinetics of folding depends on the model of dynamics
adopted for the time evolution of the system. We consider three such models:
Rouse-like dynamics with either single monomer moves or with single and double
monomer moves, and the 'slithering snake' dynamics. Usually, the snake dynamics
has poorer folding properties compared to the Rouse-like dynamics, but examples
of opposite behavior can also be found. This behavior relates to which
conformations act as local energy minima when their stability is checked
against the moves of a particular dynamics. A characteristic temperature
related to the combined probability, , to stay in the non-native minima
during folding coincides with the temperature of the fastest folding. Studies
of yield an easy numerical way to determine conditions of the optimal
folding.Comment: REVTeX, 5 pages, 6 EPS figures, to appear in J. Chem. Phy
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