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Titlebook: Enzyme Engineering; Methods and Protocol Francesca Magnani,Chiara Marabelli,Francesca Parad Book 2022 The Editor(s) (if applicable) and The

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51#
發(fā)表于 2025-3-30 09:51:00 | 只看該作者
52#
發(fā)表于 2025-3-30 13:04:58 | 只看該作者
Markku Ohenoja,Marko Paavola,Kauko Leivisk?mutagenesis, site-directed or site-saturation mutagenesis requires a semi-rational selection of the amino acid positions or the substituted residues, which can dramatically reduce the screening efforts in protein engineering. To this end, in silico prediction methods play a pivotal role in targeting
53#
發(fā)表于 2025-3-30 16:47:02 | 只看該作者
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發(fā)表于 2025-3-30 22:09:54 | 只看該作者
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發(fā)表于 2025-3-31 03:27:21 | 只看該作者
Ainor Khaliah Mohd Isa,Nurul Shahira Azuddinisclosing the evolutionary history—.., the phylogeny—of a protein family of interest and then inferring the sequences of its ancestors—.., the nodes in the phylogeny. Assisted by gene synthesis, the selected ancestors can be resurrected in the lab and experimentally characterized. The crucial step t
56#
發(fā)表于 2025-3-31 07:17:10 | 只看該作者
Manuel Ferre,Martin Buss,Carlos Balaguerand there is much interest in exploiting their functional and catalytic capabilities within minimal, de novo designed protein scaffolds. Here we describe how, using only natural biosynthetic and post-translational modification pathways, de novo designed soluble and hydrophobic proteins can be equipp
57#
發(fā)表于 2025-3-31 10:59:51 | 只看該作者
V. Adhikar,A. Karmakar,B. Biswas,C. Saharehension of the thermal stability regulating factors of proteins is needful for the engineering of their thermostability. Protein engineering aims to overcome their natural limitations in tough conditions by refining protein stability and activity. Rational-design approach requires a crystal struct
58#
發(fā)表于 2025-3-31 14:41:48 | 只看該作者
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