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Improving protein stability is an important goal for basic research as well as for clinical and industrial applications but no commonly accepted and widely used strategy for efficient engineering is known. Beside random approaches like error prone PCR or physical techniques to stabilize proteins, e.g. by immobilization, in silico approaches are gaining more attention to apply target-oriented mutagenesis. In this review different algorithms for the prediction of beneficial mutation sites to enhance protein stability are summarized and the advantages and disadvantages of FoldX are highlighted. The question whether the prediction of mutation sites by the algorithm FoldX is more accurate than random based approaches is addressed.
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O. Buß
Nuclear Energy Agency
Jens Rudat
Karlsruhe Institute of Technology
Katrin Ochsenreither
University of Applied Sciences Kaiserslautern
SHILAP Revista de lepidopterología
Computational and Structural Biotechnology Journal
Karlsruhe Institute of Technology
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Buß et al. (Mon,) studied this question.
synapsesocial.com/papers/69dd4513ac7bdbc6c71015a0 — DOI: https://doi.org/10.1016/j.csbj.2018.01.002