Alteration of T4 lysozyme structure by second-site reversion of deleterious mutations
Graduate School of Biomedical Sciences; Graduate School of Biomedical Sciences; Department of Molecular Genetics and Microbiology
Life Sciences | Medicine and Health Sciences
Mutations that suppress the defects introduced into T4 lysozyme by single amino acid substitutions were isolated and characterized. Among 53 primary sites surveyed, 8 yielded second-site revertants; a total of 18 different mutants were obtained. Most of the restorative mutations exerted global effects, generally increasing lysozyme function in a number of primary mutant contexts. Six of them were more specific, suppressing only certain specific deleterious primary substitutions, or diminishing the function of lysozymes bearing otherwise nondeleterious primary substitutions. Some variants of proteins bearing primary substitutions at the positions of Asp 20 and Ala 98 are inferred to have significantly altered structures.
Protein Sci. 1997 Nov;6(11):2418-25.
Protein science : a publication of the Protein Society
Poteete AR, Rennell D, Bouvier SE, Hardy LW. (1998). Alteration of T4 lysozyme structure by second-site reversion of deleterious mutations. GSBS Student Publications. Retrieved from https://escholarship.umassmed.edu/gsbs_sp/1001