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- W2086348548 abstract "Designing novel proteins with specific properties remains a difficult goal to achieve, mainly because the understanding of the relationship between protein sequences and certain structures or properties is still incomprehensive. For the case of mechanical proteins, even though few successes are accomplished to enhance the mechanical strengths of protein domains, there are no rational and systematic methods to design proteins with specific mechanical properties. It has been shown that the Ig-like domains in the I-band of Titin need hierarchical external forces to unfold. Dr. Braun's group analyzed the sequences of the weak and strong Ig-like domains from different species, and identified unique motifs which may be important for the hierarchical strengths of Ig-like domains. In this study,we designed four novel proteins by swapping motifs or segments from strong domain I27 to weak domain I1. The hypothesis is that the unfolding forces of the mutants will be increased. We tested their unfolding forces by single molecular Atomic Force Microscope (AFM) experiments to verify the enhancements of mechanical strengths. Preliminary data indicate that the unfolding forces of some designed mutants are increased to the level of I27. Steered Molecular Dynamics (SMD) simulations for these mutants are in process to analyze the conformational changes during unfolding. The change of backbone hydrogen bonds of A-B, A’-G strands and their side-chain interactions with neighboring residues are monitored, since they were reported to be the key determinants of mechanical strengths for Ig-like domains in titin." @default.
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- W2086348548 date "2011-02-01" @default.
- W2086348548 modified "2023-09-26" @default.
- W2086348548 title "Designing Novel Proteins with Enhanced Mechanical Strengths" @default.
- W2086348548 doi "https://doi.org/10.1016/j.bpj.2010.12.1101" @default.
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