@article {101036,
	title = {Proteins with selected sequences: A heteropolymeric study},
	journal = {Phys. Rev. E},
	volume = {62},
	year = {2000},
	month = {2000},
	pages = {7100 - 7110},
	abstract = {Protein sequences are expected not to be random but selected in order to form a stable native structure that is kinetically accessible. Therefore our model contains a selective temperature in sequence space (see [S. Ramanathan and E. Shakhnovich, Phys. Rev. E 50, 1303 (1994)] ) to optimize the sequence for the target conformation statistically. Replica calculations, which go beyond quadratic approximations in the field-theoretical Hamiltonian, are presented. A phase diagram indicating the temperatures and selective temperatures at which transitions to a frozen globule, i.e., the native state, occur is obtained. It is shown that going beyond the quadratic approximation in the field Hamiltonian is very important, since it results in a significant change of the phase diagram. Moreover, we suggest that a one-step replica permutation symmetry scheme is sufficient to solve the model. In addition to this we present a result for the sequence correlation function along the chain in the case of a short-ranged potential between the monomers. A correlation function between monomers that form a contact in the native state is given depending on the temperature and the interaction parameter.},
	url = {http://dx.doi.org/10.1103/PhysRevE.62.7100},
	author = {Wilder, J. and Shakhnovich, E.I.}
}
