Conformational dynamics of free and membrane-bound human Hsp70 in model cytosolic and endo-lysosomal environments

Autor: Valeria Calvaresi, Line T. Truelsen, Sidsel B. Larsen, Nikolaj H. T. Petersen, Thomas Kirkegaard, Kasper D. Rand

Publikováno v: Communications Biology, Vol 4, Iss 1, Pp 1-11 (2021)

Calvaresi et al. use hydrogen-deuterium exchange coupled to mass spectrometry to compare the conformational dynamics of the human heat shock protein Hsp70 when free and when associated with liposomes composed of common lysosomal lipids. They also inv

Externí odkaz: https://doaj.org/article/f5f21a3024104345a56f30bd6c1f0a41

Conformational dynamics of the human serotonin transporter during substrate and drug binding

Autor: Ingvar R. Möller, Marika Slivacka, Anne Kathrine Nielsen, Søren G. F. Rasmussen, Ulrik Gether, Claus J. Loland, Kasper D. Rand

Publikováno v: Nature Communications, Vol 10, Iss 1, Pp 1-13 (2019)

The serotonin transporter (SERT) is responsible for re-uptake of serotonin into the presynaptic neuron and plays a key role in synaptic transmission. Here, the authors use hydrogen-deuterium exchange mass spectrometry to probe the conformational dyna

Externí odkaz: https://doaj.org/article/0eff74681cb349509bf0274d56961747

Conformational heterogeneity of Savinase from NMR, HDX-MS and X-ray diffraction analysis

Autor: Shanshan Wu, Tam T.T.N. Nguyen, Olga V. Moroz, Johan P. Turkenburg, Jens E. Nielsen, Keith S. Wilson, Kasper D. Rand, Kaare Teilum

Publikováno v: PeerJ, Vol 8, p e9408 (2020)

Background Several examples have emerged of enzymes where slow conformational changes are of key importance for function and where low populated conformations in the resting enzyme resemble the conformations of intermediate states in the catalytic pr

Externí odkaz: https://doaj.org/article/38349b60495a4b6a9910ff94e5a0810f

Hydrogen–Deuterium Exchange Mass Spectrometry with Integrated Size-Exclusion Chromatography for Analysis of Complex Protein Samples

Autor: Kasper D. Rand, Andreas Redsted, Nathalie Norais, Valeria Calvaresi

Publikováno v: Calvaresi, V, Redsted, A, Norais, N & Rand, K D 2021, ' Hydrogen-Deuterium Exchange Mass Spectrometry with Integrated Size-Exclusion Chromatography for Analysis of Complex Protein Samples ', Analytical Chemistry, vol. 93, no. 33, pp. 11406–11414 . https://doi.org/10.1021/acs.analchem.1c01171

The growing use of hydrogen-deuterium exchange mass spectrometry (HDX-MS) for studying membrane proteins, large protein assemblies, and highly disulfide-bonded species is often challenged by the presence in the sample of large amounts of lipids, prot

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12087b88305adb2e31e0b0111818ffbb
https://doi.org/10.1021/acs.analchem.1c01171

Hydrogen/deuterium exchange mass spectrometry with improved electrochemical reduction enables comprehensive epitope mapping of a therapeutic antibody to the cysteine-knot containing vascular endothelial growth factor

Autor: Cornelia Wagner, Hendrik-Jan Brouwer, Kasper D. Rand, Gerard Comamala, Pablo Sanz de la Torre, Rasmus U. Jakobsen, Maximiliane Hilger

Publikováno v: Comamala, G, Wagner, C, de la Torre, P S, Jakobsen, R U, Hilger, M, Brouwer, H-J & Rand, K D 2020, ' Hydrogen/deuterium exchange mass spectrometry with improved electrochemical reduction enables comprehensive epitope mapping of a therapeutic antibody to the cysteine-knot containing vascular endothelial growth factor ', Analytica Chimica Acta, vol. 1115, pp. 41-51 . https://doi.org/10.1016/j.aca.2020.04.014

Hydrogen/deuterium exchange mass spectrometry (HDX-MS) has become a popular method for analysis of the conformational dynamics and interactions of proteins. Disulfide-bonded proteins, however, present a challenge to HDX-MS as they require efficient d

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8bc0d61cc3a40329c5d0be218d8c8f2c
https://doi.org/10.1016/j.aca.2020.04.014