Favin versus concanavalin A: Circularly permuted amino acid sequences
نویسندگان
چکیده
منابع مشابه
A transposase strategy for creating libraries of circularly permuted proteins
A simple approach for creating libraries of circularly permuted proteins is described that is called PERMutation Using Transposase Engineering (PERMUTE). In PERMUTE, the transposase MuA is used to randomly insert a minitransposon that can function as a protein expression vector into a plasmid that contains the open reading frame (ORF) being permuted. A library of vectors that express different ...
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The role that domain flexibility plays in the enzymatic activity of beta-lactamase from Staphylococcus aureus PC1 was investigated by producing two circularly permuted molecules. The C- and N-termini of the wild-type enzyme are adjacent to each other and remote from the active site, which is located between two domains. The polypeptide chain crosses over from one domain to the other twice. For ...
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Seed protein of foxtai1 and proso millets were fractionated into polypeptides that were analyzed for their major protein, prolamin, and the NHrterminal amine acid seqllenccs of the proteins were determined. The proteins extracted from foxtail and proso millets were 64.1% and 80.0% prolamin, respectively. The polypeptides of the prolamins were classMed into two groups. The majer polypeptides of ...
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We have determined the crystal structure of the GDP complex of the YjeQ protein from Thermotoga maritima (TmYjeQ), a member of the YjeQ GTPase subfamaily. TmYjeQ, a homologue of Escherichia coli YjeQ, which is known to bind to the ribosome, is composed of three domains: an N-terminal oligonucleotide/oligosaccharide-binding fold domain, a central GTPase domain, and a C-terminal zinc-finger domai...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1979
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.76.7.3218