Replacement of all tryptophan residues in T4 bacteriophage lysozyme by tyrosine residues

Inouye, Masayori; Akaboshi, Eiko; Kuroda, Mitsue; Tsugita, Akira

doi:10.1016/0022-2836(70)90104-x

Cited by 12 publications

(2 citation statements)

References 10 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Temperature-sensitive pseudorevertants of amber mutations at the positions of two tryptophans (residues 138 and 158) were from the collection of George Streisinger [see Inouye et al (1970)].…”

Section: Methodsmentioning

confidence: 99%

Temperature-sensitive mutations of bacteriophage T4 lysozyme occur at sites with low mobility and low solvent accessibility in the folded protein

Alber¹,

Sun²,

Nye³

et al. 1987

Biochemistry

263

142

View full text Add to dashboard Cite

Twenty-five different temperature-sensitive point mutations at 20 sites in the lysozyme gene of bacteriophage T4 have been identified. All of the mutations alter amino acid side chains that have lower than average crystallographic thermal factors and reduced solvent accessibility in the folded protein. This suggests that the amino acids with well-defined conformations can form specific intramolecular interactions that make relatively large contributions to the thermal stability of the protein. Residues with high mobility or high solvent accessibility are much less susceptible to destabilizing substitutions, suggesting that, in general, such amino acids contribute less to protein stability. The pattern of the sites of ts substitutions observed in the folded conformation of T4 lysozyme suggests that severe destabilizing mutations that primarily affect the free energy of the unfolded state are rare. These results indicate that proteins can be stabilized by adding new interactions to regions that are rigid or buried in the folded conformation.

show abstract

Section: Methodsmentioning

confidence: 99%

Temperature-sensitive mutations of bacteriophage T4 lysozyme occur at sites with low mobility and low solvent accessibility in the folded protein

Alber¹,

Sun²,

Nye³

et al. 1987

Biochemistry

263

142

View full text Add to dashboard Cite

show abstract

“…We note that there are 2 sets of altered suppressor mutants: one set which can suppress am eLA3 1 and one set which cannot. am eLA3 1 is a mutant of T4 lysozyme in residue 105 (glutamine) [3,4] . About half of our mutants gained the ability to suppress am eLA3 1.…”

Section: In Vivo Suppression Patterns Of the Mutant Suppressorsmentioning

confidence: 99%