Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Laetitia Denbigh"'
Autor:
Dietmar Hammerschmid, Valeria Calvaresi, Chloe Bailey, Benjamin Russell Lewis, Argyris Politis, Michael Morris, Laetitia Denbigh, Malcolm Anderson, Eamonn Reading
Lipid interactions modulate the function, folding, structure, and organization of membrane proteins. Hydrogen/deuterium exchange mass spectrometry (HDX-MS) has emerged as a useful tool to understand the structural dynamics of these proteins within li
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0b7feeaff864ee0f469c13579af8a8c
https://eprints.soton.ac.uk/478873/
https://eprints.soton.ac.uk/478873/
Autor:
Dietmar Hammerschmid, Valeria Calvaresi, Chloe Bailey, Benjamin Russell Lewis, Argyris Politis, Mike Morris, Laetitia Denbigh, Malcolm Anderson, Eamonn Reading
Lipid interactions modulate the function, folding, structure, and organization of membrane proteins. Hydrogen/deuterium exchange mass spectrometry (HDX-MS) has emerged as a useful tool to understand the structural dynamics of these proteins within li
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a15a98c479bd304728e9688be6000ef8
https://doi.org/10.26434/chemrxiv-2022-8j01g
https://doi.org/10.26434/chemrxiv-2022-8j01g
Autor:
Hassan M. Saleem, Laetitia Denbigh, Ashley S. Phillips, Cait E. MacPhee, Perdita E. Barran, Rebecca Beveridge
Publikováno v:
Proteomics
In recent years both mass spectrometry (MS) and ion mobility mass spectrometry (IM-MS) have been developed as techniques with which to study proteins that lack a fixed tertiary structure but may contain regions that form secondary structure elements
Publikováno v:
International Journal of Mass Spectrometry
International Journal of Mass Spectrometry, 2013, 354-355, pp.235-241
International Journal of Mass Spectrometry, Elsevier, 2013, 354-355, pp.235-241
International Journal of Mass Spectrometry, 2013, 354-355, pp.235-241
International Journal of Mass Spectrometry, Elsevier, 2013, 354-355, pp.235-241
Mass spectrometry was used in conjunction with ion mobility experiments and molecular modeling to study any conformational changes of two PAMAM dendrimers of different structure as a function of their protonation degree. Changes of molecular conforma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8480b100b96b6eafbd04ef39a0712665
http://hdl.handle.net/11368/2761024
http://hdl.handle.net/11368/2761024