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Computer simulation of globules with microstructure
Author(s) -
Ivanov Victor A.,
Chertovich Alexander V.,
Lazutin Alexei A.,
Shusharidezhda P.,
Khalatur Pavel G.,
Khokhlov Alexei R.
Publication year - 1999
Publication title -
macromolecular symposia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.257
H-Index - 76
eISSN - 1521-3900
pISSN - 1022-1360
DOI - 10.1002/masy.19991460135
Subject(s) - copolymer , monte carlo method , monomer , chain (unit) , sequence (biology) , membrane , protein primary structure , molecular dynamics , materials science , polymer chemistry , microstructure , statistical physics , crystallography , chemistry , computational chemistry , physics , polymer , peptide sequence , mathematics , organic chemistry , statistics , biochemistry , astronomy , gene
We present recent data of our Monte Carlo computer simulation study of properties of AB‐copolymer globules which depend strongly on the primary sequence of A and B monomeric units. Different primary sequences have been studied: random, random‐block, regular and designed ones by using some particular spatial conformation of a homopolymer chain (we have compared here three models: proteinlike copolymers, AB‐copolymers modeling membrane proteins and ABC‐copolymers modeling proteins with active enzymatic center). We have found several evidences for the fact that an AB‐copolymer chain with a primary sequence prepared on the basis of a particular conformation of a homopolymer chain by some “coloring” procedure preserves the “memory” about its “parent” spatial conformation. Analyzing the power spectra of AB‐sequences, we find the existence of long‐range power‐law correlations for the copolymers with specially designed primary sequences.