Zobrazeno 1 - 10
of 30
pro vyhledávání: '"L. Religa"'
Autor:
Alexandr Nasedkin, Moreno Marcellini, Tomasz L Religa, Stefan M Freund, Andreas Menzel, Alan R Fersht, Per Jemth, David van der Spoel, Jan Davidsson
Publikováno v:
PLoS ONE, Vol 10, Iss 5, p e0125662 (2015)
The folding and unfolding of protein domains is an apparently cooperative process, but transient intermediates have been detected in some cases. Such (un)folding intermediates are challenging to investigate structurally as they are typically not long
Externí odkaz:
https://doaj.org/article/0c69037db4244bb1b1a87aca2faf107d
Publikováno v:
Protein Science. 22:1646-1654
The low solubility of many proteins hinders large scale expression and purification as well as biophysical measurements. Here, we devised a general strategy to solubilize a protein by conjugating it at a solvent-exposed position to a 6 kDa protein th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::52462ce17debe38add2d7ed55350a2e6
https://doi.org/10.1002/pro.2337
https://doi.org/10.1002/pro.2337
Publikováno v:
Angewandte Chemie International Edition
Bigger is better: Sequential backbone assignments are obtained by NMR spectroscopy for a 1 MDa proteasome complex. The method relies on immobilization of a soluble protein complex by magic-angle spinning. Deuteration and proton detection of exchangea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c670425fc043ddd43804149b81e8dc83
https://doi.org/10.1002/anie.201301215
https://doi.org/10.1002/anie.201301215
Publikováno v:
Angewandte Chemie
Je größer, umso besser: Sequenzielle NMR-spektroskopische Zuordnungen des Proteinrückgrats gelangen für einen Proteasomkomplex von ca. 1 MDa. Die Methode beruht auf einer Immobilisierung des Komplexes durch Probenrotation im magischen Winkel. In
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2294b630f0cd6539fb7cb2a73fd39b81
https://doi.org/10.1002/ange.201301215
https://doi.org/10.1002/ange.201301215
A pulse scheme is presented for quantifying millisecond time scale chemical exchange processes in proteins by measuring (1)H CPMG relaxation dispersion profiles of (13)CHD(2) methyl groups. The use of (13)CHD(2) isotopomers for (1)H methyl dispersion
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2c39bb1547e709350ec0a6c1d28172f
https://ora.ox.ac.uk/objects/uuid:d9278129-bc31-452f-b0ba-71c89a43c79b
https://ora.ox.ac.uk/objects/uuid:d9278129-bc31-452f-b0ba-71c89a43c79b
Publikováno v:
The Journal of Physical Chemistry B. 116:6637-6644
We have recently reported the atomic resolution structure of a low populated and transiently formed on-pathway folding intermediate of the FF domain from human HYPA/FBP11 [Korzhnev, D. M.; Religa, T. L.; Banachewicz, W.; Fersht, A. R.; Kay, L.E. Scie
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff0af32e3db040f99ead9dc560fa7f56
https://doi.org/10.1021/jp209974f
https://doi.org/10.1021/jp209974f
Publikováno v:
Proceedings of the National Academy of Sciences. 108:5596-5601
Members of the homeodomain superfamily are three-helix bundle proteins whose second and third helices form a helix-turn-helix motif (HTH). Their folding mechanism slides from the ultrafast, three-state framework mechanism for the engrailed homeodomai
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ed86577ed856e5c4bb344493e2f648a
https://doi.org/10.1073/pnas.1101752108
https://doi.org/10.1073/pnas.1101752108
Publikováno v:
Science. 329:1312-1316
Transient Protein Conformations Transient conformations are important to protein function; however, detecting and characterizing these states is technically challenging. Korzhnev et al. (p. 1312 ; see the Perspective by Al-Hashimi ) combined recently
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::18e114ec61aaea2e70b2cf1b7bdec131
https://doi.org/10.1126/science.1191723
https://doi.org/10.1126/science.1191723
Publikováno v:
Journal of Molecular Biology. 371:1135-1140
CHD7 is a member of the chromodomain helicase DNA binding domain (CHD) family of ATP-dependent chromatin remodelling enzymes. It is mutated in CHARGE syndrome, a multiple congenital anomaly condition. CHD7 is one of a subset of CHD proteins, unique t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::324435750c53a717439fb5e6bfa19971
https://doi.org/10.1016/j.jmb.2007.06.007
https://doi.org/10.1016/j.jmb.2007.06.007
Autor:
Kaare Teilum, Silke Wiesner, Irina Bezsonova, Lewis E. Kay, Patrik Lundström, Mikael Akke, D. Flemming Hansen, Tomasz L. Religa, Tommy Carstensen
Publikováno v:
Journal of Biomolecular NMR. 38:199-212
A simple labeling approach is presented based on protein expression in [1-(13)C]- or [2-(13)C]-glucose containing media that produces molecules enriched at methyl carbon positions or backbone C(alpha) sites, respectively. All of the methyl groups, wi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2975c9ec1134e407362e77af27d5b44b
https://doi.org/10.1007/s10858-007-9158-6
https://doi.org/10.1007/s10858-007-9158-6