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TZID:Europe/Stockholm
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DTSTART:20170326T010000
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DTSTART:20171029T010000
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DTSTART:20190331T010000
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DTSTART:20191027T010000
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BEGIN:VEVENT
DTSTART;TZID=Europe/Stockholm:20180516T130000
DTEND;TZID=Europe/Stockholm:20180516T160000
DTSTAMP:20260504T190822
CREATED:20180315T200908Z
LAST-MODIFIED:20180316T165635Z
UID:13605-1526475600-1526486400@kemisamfundet.se
SUMMARY:HelsingborgskretsenVårvandring - projekt vildbin
DESCRIPTION:Janne Johansson guidar oss bland floran och faunan i lilla biparadiset i Örkelljunga.\nAnmälan till lerrab@telia.com
URL:https://kemisamfundet.se/event/varvandring-projekt-vildbin/
LOCATION:Örkelljunga\, Ugglestigen\, Sverige
CATEGORIES:Kretsevenemang
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Stockholm:20180521T180000
DTEND;TZID=Europe/Stockholm:20180521T180000
DTSTAMP:20260504T190822
CREATED:20180515T113454Z
LAST-MODIFIED:20180515T130852Z
UID:14251-1526925600-1526925600@kemisamfundet.se
SUMMARY:Göteborgskretsen Kafé Kemi: Periodiska systemet
DESCRIPTION:
URL:https://kemisamfundet.se/event/goteborgskretsen-kafe-kemi-periodiska-systemet/
LOCATION:Mölndals nya bibliotek\, Sverige
CATEGORIES:Kretsevenemang
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Stockholm:20180524T180000
DTEND;TZID=Europe/Stockholm:20180524T190000
DTSTAMP:20260504T190822
CREATED:20180517T105145Z
LAST-MODIFIED:20180517T105404Z
UID:14246-1527184800-1527188400@kemisamfundet.se
SUMMARY:The amyloid β peptide in Alzheimer´s disease
DESCRIPTION:Public lecture at the Chemical Society in Lund by: \nAstrid Gräslund\nProfessor of Biophysics\, Stockholm University\, Stockholm\, Sweden and\nReceiver of the Bror Holmberg medal \nTitle: “The amyloid β peptide in Alzheimer´s disease: molecular interactions and structure conversions studied by chemical and biophysical methods ” \nTime: 18:00\nPlace: Hall C\, Chemical Center\, Naturvetarvägen 14 \nAbstract\nThe amyloid β (Aβ) peptide consists of 39-43 residues and is the major component of the neuritic plaques in the brains of Alzheimer’s disease (AD) patients. It is possible to study the peptide self-aggregation process (“amyloid formation”\, structures and kinetics) using biophysical methods such as NMR\, fluorescence or CD spectroscopy. The interactions of Ab with small molecules\, or metal ions such as Zn(II) or Cu(II)\, that modulate the aggregation process can be studied in semi-stationary states by these methods (1). Kinetic effects on the amyloid formation process can be followed by fluorescence\, after labeling the material rich in β-structure by the amyloid-specific dye Thioflavin T. The β-hairpin structure of the peptide with a mainly unstructured N-terminus appears to be a basic unit for formation of the larger amyloid structures associated with insoluble fibrils. Smaller oligomeric peptide aggregates\, possibly the major cell toxic agents\, can be studied by Soft Ionization Mass Spectrometry. Fluorescence Correlation Spectroscopy (FCS) shows the heterogeneity of the aggregation process of ThT-labeled Aβ in terms of time dependent amyloid aggregate sizes\, on a single particle level (2). Modulation of the amyloid formation by Zn(II) or Cu(II) ions binding to specific residues in the N-terminus of the Aβ peptide can be followed by FCS\, showing changes in structures as well as kinetics for the aggregation process. Understanding the basic properties\, molecular interactions and reactions of the major participants in the chemical processes leading to AD gives a firm basis for the future development of agents that may be used in therapies against AD (3\,4). \nReferences:\n1. Abelein\, A.\, Gräslund\, A. and Danielsson\, J. Zinc as a chaperone-mimicking agent for retardation of amyloid β peptide fibril formation. Proc. Nat. Acad. Sci. US 112 (2015) 5407-5412.\n2. Tiiman\, A.\, Jarvet\, J.\, Gräslund\, A. and Vukojevic\, V. Heterogeneity and intermediates turnover during amyloid-β (Aβ) peptide aggregation studied by fluorescence correlation spectroscopy. Biochemistry 54 (2015) 7203-7211.\n3. Luo\, J.\, Wärmländer\, K.T.S.\, Gräslund\, A. and Abrahams\, J.P. Cross interactions between the Alzheimer disease amyloid-β peptide and other amyloid proteins: a further aspect of the amyloid cascade hypothesis. J. Biol. Chem. 291 (2016) 16485-16493.\n4. Wallin\, C.\, Luo\, J.\, Jarvet\, J.\, Wärmländer\, K.T.S. and Gräslund\, A. The amyloid β peptide in amyloid formation processes: interactions with blood proteins and naturally occurring metal ions. Israel J. Chem. 57 (SI) (2017) 674-685. \nInfo\nThe lecture is open to the public and will be held in english. After the lecture there will be an informal reception at the Centre for Analysis and Synthesis (CAS)\, where you can meet the lecturer and the other attendants. Pea soup with punsch and pancakes (50 SEK) will be served\, as well as other refreshments. \nRegister for the reception no later than Monday 21/5 by sending an e-mail to anita.hoang ’at’ chem.lu.se \nEntrance E at Naturvetarvägen 14 will be held open a short time before the lecture for visitors without access-cards. \nWelcome!
URL:https://kemisamfundet.se/event/the-amyloid-%ce%b2-peptide-in-alzheimers-disease/
LOCATION:Hall C\, Kemicentrum\, Lund\, Lunds universitet\, Lund\, 221 00\, Sverige
CATEGORIES:Kretsevenemang
ATTACH;FMTTYPE=image/png:https://kemisamfundet.se/wp-content/uploads/2018/05/Gräslund.png
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Stockholm:20180530T150000
DTEND;TZID=Europe/Stockholm:20180530T150000
DTSTAMP:20260504T190822
CREATED:20180515T114104Z
LAST-MODIFIED:20180515T153159Z
UID:14254-1527692400-1527692400@kemisamfundet.se
SUMMARY:Göteborgskretsen Studiebesök på Rise jordbruk och livsmedel
DESCRIPTION:
URL:https://kemisamfundet.se/event/goteborgskretsen-studiebesok-pa-rise-jordbruk-och-livsmedel/
CATEGORIES:Kretsevenemang
END:VEVENT
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