Random sequences with power-law correlations exhibit proteinlike behavior.
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.
Mamasakhlisov
Yevgeni Sh
YSh
Institute of Physics, Academia Sinica, Nankang, Taipei 11529, Taiwan.
Hayryan
Shura
S
Hu
Chin-Kun
CK
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
D011506:Proteins