Folding kinetics of proteins : a model study

摘要: We study the kinetics of folding a heteropolymer containing specific sequence hydrophobic, hydrophilic, and neutral residues. The heteropolymer, representing alpha carbon model protein, folds into β‐barrel structure below characteristic transition temperature. Several measures are introduced to probe dynamics approach folded state with particular emphasis on formation nonbonded contacts starting from high temperature random configuration. compactness used argue that even temperature, formed at very slow rate. This result is further corroborated by analyzing relaxation interactions which responsible for structures low temperatures. also show short times, undergoes large structural fluctuations. Examination time dependence the...