Title
Alteration of T4 lysozyme structure by second-site reversion of deleterious mutations
UMMS Affiliation
Graduate School of Biomedical Sciences; Graduate School of Biomedical Sciences; Department of Molecular Genetics and Microbiology
Publication Date
1998-02-12
Document Type
Article
Disciplines
Life Sciences | Medicine and Health Sciences
Abstract
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.
Source
Protein Sci. 1997 Nov;6(11):2418-25.
Journal/Book/Conference Title
Protein science : a publication of the Protein Society
Related Resources
PubMed ID
9385644
Repository Citation
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