## Abstract To try to resolve the loss of stability in the temperatureβsensitive mutant of T4 lysozyme, Arg 96 β His, all of the remaining 18 naturally occurring amino acids were substituted at site 96. Also, in response to suggestions that the charged residues Lys85 and Asp89, which are 5β8 Γ away
Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme
β Scribed by Alber, Tom; Dao-pin, Sun; Wilson, Keith; Wozniak, Joan A.; Cook, Sean P.; Matthews, Brian W.
- Book ID
- 109751090
- Publisher
- Nature Publishing Group
- Year
- 1987
- Tongue
- English
- Weight
- 886 KB
- Volume
- 330
- Category
- Article
- ISSN
- 0028-0836
- DOI
- 10.1038/330041a0
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Surface tension kinetics exhibited by the wild type and selected stability mutants of T4 lysozyme at the air-water interface were monitored with DuNouy tensiometry. Mutant lysozymes were produced by substitution of the isoleucine at position 3 with cysteine, leucine, glycine, and tryptophan. Each su
## Abstract The structures of three mutants of bacteriophage T4 lysozyme selected using a screen designed to identify thermostable variants are described. Each of the mutants has a substitution involving threonine. Two of the variants, Thr 26 β Ser (T26S) and Thr 151 β Ser (T151S), have increased r