Enzyme Engineering and Evolution: General Methods

<p>1. In vivo site-directed recombination (SDR): An efficient tool to reveal beneficial epistasis</p> <p>Javier Viña-Gonzalez and Miguel Alcalde</p> <p>2. A beginner's guide to molecular dynamics simulations and the identification of cross-correlation networks for enzyme engineering</p> <p>Haoran Yu and Paul A. Dalby</p> <p>3. Exploration of enzyme diversity: High-throughput techniques for protein production and microscale biochemical characterization</p> <p>Michal Vasina, Pavel Vanacek, Jiri Damborsky and Zbynek Prokop</p> <p>4. Emulsion-based directed evolution of enzymes and proteins in yeast</p> <p>Elizabeth C. Gardner, Ella J. Watkins, Jimmy Gollihar and Andrew D. Ellington</p> <p>5. Remodeling enzyme active sites by stepwise loop insertion</p> <p>Md Anarul Hoque, Yong Zhang, Li Zhi, Li Cui and Yan Feng</p> <p>6. Consensus Finder web tool to predict stabilizing substitutions in proteins</p> <p>Bryan J. Jones, Chi Nok Enoch Kan, Christine Luo and Romas J. Kazlauskas</p> <p>7. The use of consensus sequence information to engineer stability and activity in proteins</p> <p>Matt Sternke, Katherine W. Tripp and Doug Barrick</p> <p>8. Structure-guided rational design of the substrate specificity and catalytic activity of an enzyme</p> <p>Jung Min Choi and Hak-Sung Kim</p> <p>9. Biological fitness landscapes by deep mutational scanning</p> <p>Jacob D. Mehlhoff and Marc Ostermeier</p> <p>10. Focused rational iterative site-specific mutagenesis (FRISM)</p> <p>Danyang Li, Qi Wu and Manfred T. Reetz</p> <p>11. Statistical analysis of mutational epistasis to reveal intramolecular interaction networks in proteins</p> <p>Charlotte M. Miton, John Z. Chen, Kalum Ost, Dave W. Anderson and Nobuhiko Tokuriki</p> <p>12. Machine learning-assisted enzyme engineering</p> <p>Niklas E. Siedhoff, Ulrich Schwaneberg and Mehdi D. Davari</p> <p>13. Ultrahigh throughput screening for enzyme function in droplets</p> <p>Stefanie Neun, Paul J. Zurek, Tomasz S. Kaminski and Florian Hollfelder</p>