Zobrazeno 1 - 10
of 168
pro vyhledávání: '"V.T. Forsyth"'
Publikováno v:
'Acta Crystallographica D ', vol: 77, pages: 1579-1590 (2021)
Ramos, J, Laux, V, Haertlein, M, Forsyth, V T, Mossou, E, Larsen, S & Langkilde, A E 2021, ' The impact of folding modes and deuteration on the atomic resolution structure of hen egg-white lysozyme ', Acta crystallographica Section D: Structural biology, vol. 77, no. 12, pp. 1579-1590 . https://doi.org/10.1107/S2059798321010950
Acta Crystallographica. Section D, Structural Biology
Ramos, J, Laux, V, Haertlein, M, Forsyth, V T, Mossou, E, Larsen, S & Langkilde, A E 2021, ' The impact of folding modes and deuteration on the atomic resolution structure of hen egg-white lysozyme ', Acta crystallographica Section D: Structural biology, vol. 77, no. 12, pp. 1579-1590 . https://doi.org/10.1107/S2059798321010950
Acta Crystallographica. Section D, Structural Biology
A study of in vitro refolding and isotope effects on protein structure, activity and stability shows that different folding dynamics can lead to important changes in protein properties.
The biological function of a protein is intimately related
The biological function of a protein is intimately related
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::082ff1ad2dc9755439d789a6869b8a3d
https://epn-library.esrf.fr/flora/jsp/index_view_direct_anonymous.jsp?record=doc:PUB_ILL:31577
https://epn-library.esrf.fr/flora/jsp/index_view_direct_anonymous.jsp?record=doc:PUB_ILL:31577
Autor:
Jane L. Ward, V.T. Forsyth, Johnjoe McFadden, Celia W. Goulding, D.J.V. Beste, Michael Haertlein, Khushboo Borah, Martine Moulin, Gernot Strohmeier, Stephan Noack, Michael H. Beale, Harald Pichler, Gerald Larrouy-Maumus, Tom A. Mendum, Apoorva Bhatt, Nathaniel D. Hawkins
The utilisation of multiple host-derived carbon substrates is required by Mycobacterium tuberculosis (Mtb) to successfully sustain a tuberculosis infection thereby identifying the Mtb specific metabolic pathways and enzymes required for carbon co-met
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::223bb941b0ebd9e8e6213f1166f5d242
https://doi.org/10.1101/2021.01.29.428863
https://doi.org/10.1101/2021.01.29.428863
Autor:
Tilo Seydel, Briony A. Yorke, Stephan Niebling, Arwen R. Pearson, Nils Huse, Raskar T, Juliette M. Devos, V.T. Forsyth, Härtlein M
Incoherent neutron spectroscopy, in combination with dynamic light scattering was used to investigate the effect of ligand binding on the center-of-mass self-diffusion and internal diffusive dynamics ofE.coliaspartateα-decarboxylase (ADC). The X-ray
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::95bb18e162f56c5ba02a26d1df71c530
https://doi.org/10.1101/2020.08.11.244939
https://doi.org/10.1101/2020.08.11.244939
Akademický článek
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Publikováno v:
Journal of Colloid and Interface Science
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=r3c4b2081b22::d99e3eb22054fb68721c43770935a4d8
Akademický článek
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Autor:
Catherine J. Merrick, Anne L. Martel, Lionel Porcar, V.T. Forsyth, A. Jordan, Mark Jacques, J. Devos
Publikováno v:
'Journal of Applied Crystallography ', vol: 49, pages: 2015-2020 (2016)
The first implementation and use of an in situ size exclusion chromatography (SEC) system on a small-angle neutron scattering instrument (SANS) is described. The possibility of deploying such a system for biological solution scattering at the Institu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17666315e630ffecf7a322d0aa0ea045
https://doi.org/10.1107/s1600576716016514
https://doi.org/10.1107/s1600576716016514
Autor:
V.T. Forsyth, Peter C. E. Moody
Publikováno v:
Acta Crystallographica Section D Structural Biology
'No abstract'
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::19bd0c1d799ed9cbf612a83b4631bc54
Akademický článek
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Autor:
Martine Moulin, A. Martel, Orla M. Dunne, M. Weidenhaupt, V.T. Forsyth, Stephen J. Perkins, P. Callow, Michael Haertlein
Publikováno v:
European Biophysics Journal
European Biophysics Journal, Springer Verlag (Germany), 2017, 46 (5), pp.425-432. ⟨10.1007/s00249-016-1186-2⟩
European Biophysics Journal, Springer Verlag (Germany), 2017, 46 (5), pp.425-432. ⟨10.1007/s00249-016-1186-2⟩
Small-angle neutron scattering (SANS) is a powerful technique for the characterisation of macromolecular structures and interactions. Its main advantage over other solution state approaches is the ability to use D2O/H2O solvent contrast variation to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29d7a25e04365c8c1806413e586ab538
https://hal.archives-ouvertes.fr/hal-01762233
https://hal.archives-ouvertes.fr/hal-01762233