Conformational selection and adaptation to ligand binding in T4 lysozyme cavity mutants

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 110; no. 46; pp. E4306 - E4315
• Main Authors: López, Carlos J., Yang, Zhongyu, Altenbach, Christian, Hubbell, Wayne L.
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 12.11.2013; National Acad Sciences
• Series: PNAS Plus
• Subjects: Anesthesia; Bacteriophage T4 - enzymology; Biological Sciences; Crystal structure; Electron Spin Resonance Spectroscopy; general anesthetics; halothane; Hydrostatic pressure; Ligands; lysozyme; Models, Molecular; Muramidase - chemistry; Muramidase - genetics; Muramidase - metabolism; Mutagenesis, Site-Directed; Mutants; Mutation; Mutation, Missense - genetics; PNAS Plus; Protein Binding; Protein Conformation; protein engineering; Proteins; spectroscopy; Spin Labels; DEER; saturation recovery; site-directed spin labeling; EPR; benzene

The studies presented here explore the relationship between protein packing and molecular flexibility using ligand-binding cavity mutants of T4 lysozyme. Although previously reported crystal structures of the mutants investigated show single conformations that are similar to the WT protein, site-dir...