Faculty Opinions recommendation of Design of a novel globular protein fold with atomic-level accuracy.

By P. Balaram. 2003

835 citations recorded by the source corpus.

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In Molecular Biology

Citations in the corpus

RosettaRemodel: A Generalized Framework for Flexible Backbone Protein Design (2011, background): “and a very stable protein with a novel protein fold”
De novo design of covalently constrained mesosize protein scaffolds with unique tertiary structures (2017, methodology): “We then used Rosetta’s fixed backbone side chain design application (48) to redesign the sequence for more compact hydrophobic core packing as well as to reduce the hydrophilicity of 3H1.”
Design of an HA2-based Escherichia coli expressed influenza immunogen that protects mice from pathogenic challenge (2010, methodology): “Using the software RosettaDesign (24), mutations were chosen to remove exposed hydrophobic patches generated due to interactions lost with the rest of HA.”
OptCDR: a general computational method for the design of antibody complementarity determining regions for targeted epitope binding. (2010, background): “While there exist a large number of protein engineering methods, only a relative small number have successfully achieved the de novo design of proteins and enzymes for a particular task (Kraemer-Pecore et al., 2003; Kuhlman et al., 2003; Offredi et al., 2003; Bender et al., 2007).”
Assessing computational methods for predicting protein stability upon mutation: good on average but not in the details. (2009, methodology): “Some of the studied methods (e.g. EGAD, FoldX, and Rosetta) were successfully applied to design new folds, improving protein stability or binding specificity (Kuhlman et al., 2003; Kortemme et al., 2004; Pokala and Handel, 2005; Szczepek et al., 2007).”