High-throughput molecular dynamics simulations: Long and short range effects of mutations on substrate specificity
暂无分享,去创建一个
Natalia Currle-Linde | Jürgen Pleiss | Peggy Lindner | Rolf D. Schmid | Fabian Bös | J. Pleiss | R. Schmid | Fabian Bös | P. Lindner | N. Currle-Linde
[1] B. Shoichet,et al. An ultrahigh resolution structure of TEM-1 beta-lactamase suggests a role for Glu166 as the general base in acylation. , 2002, Journal of the American Chemical Society.
[2] T. Palzkill,et al. Molecular analysis of beta-lactamase structure and function. , 2002, International journal of medical microbiology : IJMM.
[3] R D Schmid,et al. Stereoselectivity of Pseudomonas cepacia lipase toward secondary alcohols: A quantitative model , 2000, Protein science : a publication of the Protein Society.
[4] I. Massova,et al. Effects on Substrate Profile by Mutational Substitutions at Positions 164 and 179 of the Class A TEMpUC19 β-Lactamase from Escherichia coli* , 1999, The Journal of Biological Chemistry.
[5] P. Bradford. Extended-Spectrum β-Lactamases in the 21st Century: Characterization, Epidemiology, and Detection of This Important Resistance Threat , 2001, Clinical Microbiology Reviews.
[6] J. Frère,et al. Catalytic properties of class A beta-lactamases: efficiency and diversity. , 1998, The Biochemical journal.
[7] Jürgen Pleiss,et al. A Molecular Mechanism of Enantiorecognition of Tertiary Alcohols by Carboxylesterases , 2003, Chembiochem : a European journal of chemical biology.
[8] Lars Ridder,et al. Identification of Glu166 as the general base in the acylation reaction of class A beta-lactamases through QM/MM modeling. , 2003, Journal of the American Chemical Society.
[9] P. Kollman,et al. A Second Generation Force Field for the Simulation of Proteins, Nucleic Acids, and Organic Molecules , 1995 .