Zobrazeno 1 - 10
of 150
pro vyhledávání: '"Thomas E. Creighton"'
Autor:
Thomas E. Creighton
Publikováno v:
Current Biology. 7:R380-R383
A major question about protein folding is whether the coming together by diffusion of different segments of the polypeptide chain is rate-determining. This seemingly simple question has been very difficult to answer experimentally, but a positive res
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1427762970901a9026f50df05f91f253
https://doi.org/10.1016/s0960-9822(06)00180-1
https://doi.org/10.1016/s0960-9822(06)00180-1
Publikováno v:
Journal of Molecular Biology. 257:188-198
The disulphide folding pathway of bovine pancreatic trypsin inhibitor (BPTI) revealed that the native conformation is still stable in each intermediate state with two native disulphide linkages, in the absence of each of the corresponding third disul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7cdc2247c7aef00944200cea79285b6b
https://doi.org/10.1006/jmbi.1996.0155
https://doi.org/10.1006/jmbi.1996.0155
Publikováno v:
The FASEB Journal. 10:110-118
Proteins can fold very rapidly, undoubtedly because they do not do so simply by random searching. The stable, partly folded species that can be detected during protein refolding are, however, of uncertain kinetic significance. The available kinetic e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::513d1ccb03e7111966de4aa247bb9596
https://doi.org/10.1096/fasebj.10.1.8566531
https://doi.org/10.1096/fasebj.10.1.8566531
Publikováno v:
Biochemistry. 35:14503-14511
Proteins with the thioredoxin fold have widely differing stabilities of the disulfide bond that can be formed between the two cysteines at their active site sequence motif Cys1-Xaa2-Yaa3-Cys4. This is believed to be regulated not by varying the disul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac3e13379f63fb31dc981ba539ba6ad5
https://doi.org/10.1021/bi9617724
https://doi.org/10.1021/bi9617724
Publikováno v:
Protein Science. 4:2587-2593
A genetically engineered protein consisting of the 120 residues at the N-terminus of human protein disulfide isomerase (PDI) has been characterized by 1H, 13C, and 15N NMR methods. The sequence of this protein is 35% identical to Escherichia coli thi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::362e69f731d47a3e551df3074b9bb4d8
https://doi.org/10.1002/pro.5560041216
https://doi.org/10.1002/pro.5560041216
Autor:
Tanja Kortemme, Thomas E. Creighton
Publikováno v:
Journal of Molecular Biology. 253:799-812
The physical basis of the unusually low pKa values of an active site cysteine thiol group in proteins with the thioredoxin fold is unknown. The electrostatic field associated with an alpha-helix pointing with its N terminus towards the cysteine resid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6ffdc96f1ffa1e5ad0091e4857a6244
https://doi.org/10.1006/jmbi.1995.0592
https://doi.org/10.1006/jmbi.1995.0592
Autor:
Thomas E. Creighton, Nigel J. Darby
Publikováno v:
Biochemistry. 34:11725-11735
The two thioredoxin-like domains of human protein disulfide isomerase (PDI) have been produced in bacteria as individual soluble, folded protein molecules, and their functional properties have been compared to those of intact PDI. The two individual
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b7590ca7eed68a5748e8bc0e5751a56
https://doi.org/10.1021/bi00037a009
https://doi.org/10.1021/bi00037a009
Publikováno v:
Biochemistry. 34:5075-5089
DsbC is a soluble protein of the bacterial periplasm that was identified genetically as being involved in protein disulfide formation. The gene sequence was corrected to include an additional proline residue and was then consistent with the molecular
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::020faed81c8a4d882cbb081709fd4430
https://doi.org/10.1021/bi00015a019
https://doi.org/10.1021/bi00015a019
Autor:
Nigel J. Darby, Thomas E. Creighton
Publikováno v:
Biochemistry. 34:3576-3587
The mechanism of action of the bacterial periplasm protein DsbA in introducing disulfide bonds into proteins was studied by its action on a model disordered peptide containing only two cysteine residues. Most of the reactions between the various thio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e72ae75a1d01329f6505fc62a88a81b2
https://doi.org/10.1021/bi00011a012
https://doi.org/10.1021/bi00011a012
Publikováno v:
Current Biology. 4:1026-1029
The crystal structure of bacteriophage P22 tailspike protein reveals a striking fold with a distinctive, fish-like appearance, and helps explain many of the properties of this unusual molecule and its folding pathway.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ab5c3d855adc25d66f07c503d5c7205
https://doi.org/10.1016/s0960-9822(00)00234-7
https://doi.org/10.1016/s0960-9822(00)00234-7