Zobrazeno 1 - 10
of 126
pro vyhledávání: '"disulphide bridge"'
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 2017 Mar . 114(13), 3415-3420.
Externí odkaz:
https://www.jstor.org/stable/26480339
Autor:
Lila Yang, Maria Hansen Falkesgaard, Peter Waaben Thulstrup, Peter Schledermann Walmod, Leila Lo Leggio, Kim Krighaar Rasmussen
Publikováno v:
PeerJ, Vol 5, p e3550 (2017)
The fibronectin leucine rich transmembrane (FLRT) protein family consists in humans of 3 proteins, FLRT1, -2, and -3. The FLRT proteins contain two extracellular domains separated by an unstructured linker. The most membrane distal part is a leucine
Externí odkaz:
https://doaj.org/article/abc5b4b188e74a84b56802b26b001af5
Publikováno v:
CHIMIA, Vol 55, Iss 12 (2001)
The disulphide-bridge pattern of the CSTX-9 polypeptide present in the multicomponent venom of the spider Cupiennius salei was determined de novo by nano-electrospray tandem mass spectrometry. Cleavage of native CSTX-9 with immobilized trypsin result
Externí odkaz:
https://doaj.org/article/825044e1a8b247c69221afd03fc66045
Autor:
K.K. Rasmussen, Peter S. Walmod, Leila Lo Leggio, Lila Yang, Maria Hansen Falkesgaard, Peter W. Thulstrup
Publikováno v:
PeerJ, Vol 5, p e3550 (2017)
Yang, L, Falkesgaard, M H, Thulstrup, P W, Walmod, P S, Lo Leggio, L & Rasmussen, K K 2017, ' Expression, refolding and spectroscopic characterization of fibronectin type III (FnIII)-homology domains derived from human fibronectin leucine rich transmembrane protein (FLRT)-1,-2, and-3 ', PeerJ, vol. 5, e3550 . https://doi.org/10.7717/peerj.3550
PeerJ
Yang, L, Falkesgaard, M H, Thulstrup, P W, Walmod, P S, Lo Leggio, L & Rasmussen, K K 2017, ' Expression, refolding and spectroscopic characterization of fibronectin type III (FnIII)-homology domains derived from human fibronectin leucine rich transmembrane protein (FLRT)-1,-2, and-3 ', PeerJ, vol. 5, e3550 . https://doi.org/10.7717/peerj.3550
PeerJ
The fibronectin leucine rich transmembrane (FLRT) protein family consists in humans of 3 proteins, FLRT1, -2, and -3. The FLRT proteins contain two extracellular domains separated by an unstructured linker. The most membrane distal part is a leucine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7cdac6c8a9bbf30561e6c0bb3ab8b99e
https://peerj.com/articles/3550/
https://peerj.com/articles/3550/
Autor:
Danilo Mourelle, João Ruggiero Neto, Patricia Brigatte, Paulo César Gomes, Nathalia Baptista Dias, Rodrigo G. Stábeli, Marcia Perez dos Santos Cabrera, Bibiana Monson de Souza, Mario Sergio Palma, Helen Andrade Arcuri
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1840:170-183
Background The peptide Paulistine was isolated from the venom of wasp Polybia paulista. This peptide exists under a natural equilibrium between the forms: oxidised — with an intra-molecular disulphide bridge; and reduced — in which the thiol grou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b3245a0120fa8a72e5711a534460ce0
https://doi.org/10.1016/j.bbagen.2013.08.024
https://doi.org/10.1016/j.bbagen.2013.08.024
Publikováno v:
Voutilainen, S P, Nurmi-Rantala, S, Penttilä, M & Koivula, A 2014, ' Engineering chimeric thermostable GH7 cellobiohydrolases in Saccharomyces cerevisiae ', Applied Microbiology and Biotechnology, vol. 98, no. 7, pp. 2991-3001 . https://doi.org/10.1007/s00253-013-5177-2
We report here the effect of adding different types of carbohydrate-binding modules (CBM) to a single-module GH7 family cellobiohydrolase Cel7A from a thermophilic fungus Talaromyces emersonii (TeCel7A). Both bacterial and fungal CBMs derived from fa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7edb2e16b022a3f53216d51520f84a44
https://doi.org/10.1007/s00253-013-5177-2
https://doi.org/10.1007/s00253-013-5177-2
Autor:
Michael Hummel, Ossi Turunen, Hairong Xiong, Heikki Ojamo, He Li, Anna Kankaanpää, Herbert Sixta
Publikováno v:
ENZYME AND MICROBIAL TECHNOLOGY. 53(6-7):414-419
In the present study, an extremophilic GH11 xylanase was stabilized by an engineered N-terminal disulphide bridge. The effect of the stabilization was then tested against high temperatures and in the presence of a biomass-dissolving ionic liquid, 1-e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae2aab1a31f56c77f14ca265f63eb2db
http://juuli.fi/Record/0336860413
http://juuli.fi/Record/0336860413
Publikováno v:
Journal of molecular catalysis. B, Enzymatic
82 (2012): 109–114. doi:10.1016/j.molcatb.2012.05.024
info:cnr-pdr/source/autori:Ordu, Emel B.; Yelboga, Emrah; Secundo, Francesco; Sessions, Richard B.; Karaguler, Nevin Gul/titolo:The effect of methionine to cysteine substitution on the stability of formate dehydrogenase from Candida methylica/doi:10.1016%2Fj.molcatb.2012.05.024/rivista:Journal of molecular catalysis. B, Enzymatic (Print)/anno:2012/pagina_da:109/pagina_a:114/intervallo_pagine:109–114/volume:82
82 (2012): 109–114. doi:10.1016/j.molcatb.2012.05.024
info:cnr-pdr/source/autori:Ordu, Emel B.; Yelboga, Emrah; Secundo, Francesco; Sessions, Richard B.; Karaguler, Nevin Gul/titolo:The effect of methionine to cysteine substitution on the stability of formate dehydrogenase from Candida methylica/doi:10.1016%2Fj.molcatb.2012.05.024/rivista:Journal of molecular catalysis. B, Enzymatic (Print)/anno:2012/pagina_da:109/pagina_a:114/intervallo_pagine:109–114/volume:82
Because of its industrial importance. the FDH enzyme has been subjected to several protein engineering studies in order to stabilise it at high temperatures. In this study, methionine to cysteine substitution (M1C) and disulphide bridge formation bet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb119e48649e34c10fede47c5fd88a59
https://doi.org/10.1016/j.molcatb.2012.05.024
https://doi.org/10.1016/j.molcatb.2012.05.024