A linker of the proline-threonine repeatingmotif sequence is bimodal. SKAF, Munir Salomão; POLIKARPOV, Igor; STANKOVIC, Ivana M.
Abstract: The linker of the endoglucanase from Xanthomonas campestris pv. campestris ((PT)12) has a specific sequence, a repeating proline-threonine motif. In order to understand its role, it has been compared to a regular sequence linker, in this work - the cellobiohydrolase 2 from Trichoderma reesei (CBH2). Elastic properties of the two linkers have been estimated by calculating free energy profile along the linker length from an enhanced sampling molecular dynamics simulation. The (PT)12 exhibits more pronounced elastic behaviour than CBH2. The PT repeating motif results in a two-mode energy profile which could be very useful in the enzyme motions along the substrate during hydrolytic catalysis.
Journal of Molecular Modeling
v. 26, n. 8, p. 178-1-178-7 - Ano: 2020
Fator de Impacto: 1,346
@article={002999910,author = {SKAF, Munir Salomão; POLIKARPOV, Igor; STANKOVIC, Ivana M.},title={A linker of the proline-threonine repeatingmotif sequence is bimodal},journal={Journal of Molecular Modeling},note={v. 26, n. 8, p. 178-1-178-7},year={2020}}
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