Zobrazeno 1 - 10
of 179
pro vyhledávání: '"Paul M. Horowitz"'
Publikováno v:
Biochemistry. 41:12843-12849
We investigated the dissociation of single-ring heptameric GroEL (SR1) by high hydrostatic pressure in the range of 1-2.5 kbar. The kinetics of the dissociation of SR1 in the absence and presence of Mg2+, KCl, and nucleotides were monitored using lig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97c99007fa5025348bbe1851cbd0c877
https://doi.org/10.1021/bi020366j
https://doi.org/10.1021/bi020366j
Publikováno v:
Archives of Biochemistry and Biophysics. 403:63-70
The molecular chaperone DnaK and trigger factor (TF), a ribosome-associated protein with folding activity, have been implicated in assisting nascent polypeptides to acquire a three-dimensional structure on Escherichia coli ribosomes. We asked whether
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::753b9d48670296c36df0d914617d8f52
https://doi.org/10.1016/s0003-9861(02)00213-8
https://doi.org/10.1016/s0003-9861(02)00213-8
Publikováno v:
Biochemistry. 41:2421-2428
Molecular chaperones GroEL and GroES facilitate reactivation of denatured rhodanese which folds poorly unless the process is assisted. The present work tests the hypothesis that more extensively unfolded forms of rhodanese bind tighter than those for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ddca09f2d2d13354a3018e9716773599
https://doi.org/10.1021/bi0115378
https://doi.org/10.1021/bi0115378
Publikováno v:
FEBS Letters. 512:209-212
The coding sequence for chloramphenicol acetyl transferase (CAT) contains several rare codons; three of them are ATA encoding isoleucine in positions 13, 84 and 119 of the amino acid sequence. Expression of CAT on Escherichia coli ribosomes in vitro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2dbf83e42e0fd879440fbbf39316cdb2
https://doi.org/10.1016/s0014-5793(02)02261-5
https://doi.org/10.1016/s0014-5793(02)02261-5
Autor:
Paul M. Horowitz, Markandeswar Panda
Publikováno v:
Biochemistry. 41:1869-1876
We investigated the dissociation of tetradecameric GroEL by high hydrostatic pressure in the range of 1-2.5 kbar. Kinetics of the dissociation of GroEL in the absence and presence of Mg(2+) and/or KCl were monitored using light scattering. All of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd59c5781efcbe11b8931251b8011ed3
https://doi.org/10.1021/bi011794c
https://doi.org/10.1021/bi011794c
Publikováno v:
Journal of Biological Chemistry. 276:28739-28743
The in vitro folding of rhodanese involves a competition between formation of properly folded enzyme and off-pathway inactive species. Co-solvents like glycerol or low temperature, e.g. refolding at 10 degrees C, successfully retard the off-pathway f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c964a73b6921929be3565757fa36f7e6
https://doi.org/10.1074/jbc.m102500200
https://doi.org/10.1074/jbc.m102500200
Autor:
and Alan R. Fersht, Alison L. Smoot, Markandeswar Panda, Bill T. Brazil, Ashley M. Buckle, Paul M. Horowitz
Publikováno v:
Biochemistry. 40:4484-4492
The extent of hydrophobic exposure upon bis-ANS binding to the functional apical domain fragment of GroEL, or minichaperone (residues 191-345), was investigated and compared with that of the GroEL tetradecamer. Although a total of seven molecules of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7838cc4955d6256b9e6793e68f174b79
https://doi.org/10.1021/bi001822b
https://doi.org/10.1021/bi001822b
Publikováno v:
Journal of Biological Chemistry. 275:63-70
The competition between protein aggregation and folding has been investigated using rhodanese (thiosulfate:cyanide sulfurtransferase, EC 2.8.1.1) as a model. During folding from a urea-denatured state, rhodanese rapidly forms associated species or in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b02f90e4c918a25232f9a6c32869a2dc
https://doi.org/10.1074/jbc.275.1.63
https://doi.org/10.1074/jbc.275.1.63
Publikováno v:
Proceedings of the National Academy of Sciences. 96:2682-2686
The interaction of the chaperonin GroEL 14 with its cochaperonin GroES 7 is dynamic, involving stable, asymmetric 1:1 complexes (GroES 7 ⋅GroEL 7 –GroEL 7 ) and transient, metastable symmetric 2:1 complexes [GroES 7 ⋅GroEL 7 –GroEL 7 ⋅GroES
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2cc5d9b3e521442d577bc142decc9d0
https://doi.org/10.1073/pnas.96.6.2682
https://doi.org/10.1073/pnas.96.6.2682
Autor:
Paul M. Horowitz, Boris M. Gorovits
Publikováno v:
Biochemistry. 37:6132-6135
The present work demonstrates that high hydrostatic pressure can increase protein folding by reducing nonspecific aggregation. Protein aggregation is one of the main side reactions that competes with protein folding, and it typically results from int
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f1222a72a40af54822618dd754acba7
https://doi.org/10.1021/bi9730137
https://doi.org/10.1021/bi9730137