title: Random sequences with power-law correlations exhibit proteinlike behavior.
abstract: We use a replica approach to investigate the thermodynamic properties of the random heteropolymers with persistent power-law correlations in monomer sequence. We show that this type of sequences possess proteinlike properties. In particular, we show that they can fold into stable unique three-dimensional structure (the "native" structure, in protein terminology) through two different types of pathways. One is a fast folding pathway and leads directly to the native structure. Another one, a more slower pathway, passes through the microphase separated (MPS) state and includes a number of intermediate glassy states. The scale and the magnitude of the MPS are calculated. The frozen state can be reached only by sequences with weak long-range correlations. The critical value for the correlation exponent is found, above which (strong correlations) freezing is impossible.
authors: Institute of Physics, Academia Sinica, Nankang, Taipei 11529, Taiwan.
authors: Yevgeni Sh
authors: YSh
authors: Mamasakhlisov
authors: Shura
authors: S
authors: Hayryan
authors: Chin-Kun
authors: CK
authors: Hu
mesh_terms: D000465:Algorithms; D000595:Amino Acid Sequence; D040761:Biomimetic Materials / Q000737:chemistry*; D003198:Computer Simulation; D008956:Models, Chemical; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D020539:Sequence Analysis, Protein / Q000379:methods*; D013223:Statistics as Topic; D013329:Structure-Activity Relationship
chemical_list: D011506:Proteins