Point mutation of alanine (31) to valine prohibits the folding of reduced lysozyme by sulfhydryl-disulfide interchange.

doi:10.1093/protein/1.4.333

Back to search

Article

Point mutation of alanine (31) to valine prohibits the folding of reduced lysozyme by sulfhydryl-disulfide interchange.

Protein engineering - 1 Jan 2000

Imoto T, Yamada H, Yasukochi T, Yamada E, Ito Y, Ueda T, Nagatani H, Miki T, Horiuchi T

Abstract excerpt

In the preceding paper in this issue, we described the overproduction of one mutant chicken lysozyme in Escherichia coli. Since this lysozyme contained two amino acid substitutions (Ala31----Val and Asn106----Ser) in addition to an extra methionine residue at the NH2-terminus, the substituted ami...

Topics

Alanine
DNA
Disulfides
Escherichia coli
Gene Expression Regulation
Muramidase
Mutation
Oxidation-Reduction
Plasmids
Sulfhydryl Compounds
Valine

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.