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Updated: Dec 17, 2025

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
Published on: July 14, 2015
A linker of the proline-threonine repeating motif sequence is bimodal
Munir Salomão Skaf1, Igor Polikarpov2, Ivana M Stanković3,4
1Institute of Chemistry, University of Campinas - UNICAMP, P.O. Box 6154, Campinas, SP, 130820864, Brazil.
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.
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