Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Liliana Falzon"'
Publikováno v:
The Journal of Biochemistry. 167:473-482
Nascent polypeptides are synthesized on ribosomes starting at the N-terminus and simultaneously begin to fold during translation. We constructed N-terminal fragments of prosubtilisin E containing an intramolecular chaperone (IMC) at N-terminus to mim
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec445b2f9ecdf53ef4a8300630f12620
https://doi.org/10.1093/jb/mvaa004
https://doi.org/10.1093/jb/mvaa004
Publikováno v:
Journal of Molecular Biology. 366:494-503
The 77 residue propeptide at the N-terminal end of subtilisin E plays an essential role in subtilisin folding as a tailor-made intramolecular chaperone. Upon completion of folding, the propeptide is autoprocessed and removed by subtilisin digestion.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c4ad38952c89059adc56ff5104bfdeb
https://doi.org/10.1016/j.jmb.2006.11.019
https://doi.org/10.1016/j.jmb.2006.11.019
Autor:
Liliana Falzon, Victor L. Davidson
Publikováno v:
Biochemistry. 35:2445-2452
The reaction of trimethylamine dehydrogenase (TMADH) with trimethylamine has been studied by rapid-scanning stopped-flow spectroscopy and steady-state kinetics. The covalently bound 6-S-cysteinylflavin mononucleotide (FMN) cofactor is initially reduc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b655980c97bf283a133fae7d08c1e040
https://doi.org/10.1021/bi951550q
https://doi.org/10.1021/bi951550q
Autor:
Victor L. Davidson, Liliana Falzon
Publikováno v:
Biochemistry. 35:12111-12118
Within the enzyme trimethylamine dehydrogenase [TMADH], intramolecular electron transfer occurs between a fully reduced covalently bound 6-S-cysteinylflavin [FMN] cofactor, and an oxidized iron-sulfur [4Fe-4S]2+ center. When the enzyme is reduced by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3661bb2ef113d0f5224c68515e778b6
https://doi.org/10.1021/bi960664e
https://doi.org/10.1021/bi960664e
Here we report the backbone chemical shifts of the DFP-inhibited mature subtilisin E, which was uniformly labeled by (13)C, (15)N with a supplement of excess calcium.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f336f2cf145cf6716162803b4bfc9ce5
https://europepmc.org/articles/PMC3197784/
https://europepmc.org/articles/PMC3197784/
Publikováno v:
The Journal of biological chemistry. 282(36)
The HAMP domain plays an essential role in signal transduction not only in histidine kinase but also in a number of other signal-transducing receptor proteins. Here we expressed the EnvZ HAMP domain (Arg(180)-Thr(235)) with the R218K mutation (termed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::060e5b2aacdab9ca1de83da48a357a42
https://pubmed.ncbi.nlm.nih.gov/17635923
https://pubmed.ncbi.nlm.nih.gov/17635923
Publikováno v:
Current opinion in biotechnology. 17(4)
An ultimate goal for any protein production system is to express only the protein of interest without producing other cellular proteins. To date, there are only two established methods that will allow the successful expression of only the protein of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::27175c26a35148c84df670b387f84196
https://pubmed.ncbi.nlm.nih.gov/16828276
https://pubmed.ncbi.nlm.nih.gov/16828276
Publikováno v:
Biochimica et biophysica acta. 1749(1)
Subtilisin E, a serine protease from Bacillus subtilis, requires an N-terminal propeptide for its correct folding. The propeptide is autocleaved and digested by the subtilisin domain upon proper folding. Here we investigated the individual roles of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c34cf924d338409a600249ebba4c03fe
https://pubmed.ncbi.nlm.nih.gov/15848132
https://pubmed.ncbi.nlm.nih.gov/15848132
Publikováno v:
Journal of biochemical and biophysical methods. 29(3-4)
The preparation and purification of PCR generated DNA fragments suitable for footprinting and classical drug binding studies is described. One of the fragments, a 214-mer derived from pBR322 DNA exhibits a biphasic melting profile. This behavior appe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::142f5422bf5787c7b0bc0683d7114fd1
https://pubmed.ncbi.nlm.nih.gov/7699202
https://pubmed.ncbi.nlm.nih.gov/7699202