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SUMMARY:Contr. talk - Aquaporins – expression\, purification and charact
 erization
DTSTART;VALUE=DATE-TIME:20210525T113500Z
DTEND;VALUE=DATE-TIME:20210525T115500Z
DTSTAMP;VALUE=DATE-TIME:20260722T083934Z
UID:indico-contribution-182-1130@lindico453.srv.lu.se
DESCRIPTION:Speakers: Kristina Hedfalk ()\nAquaporin water channels facili
 tate the bi-directional flow of water and small\, neutral solutes down an 
 osmotic gradient in all kingdoms of life. Over the last two decades\, the 
 availability of\nhigh-quality protein has underpinned progress in the stru
 ctural and functional characterization of these water channels. In particu
 lar\, recombinant protein technology has guaranteed the supply of aquapori
 n samples that were of sufficient quality and quantity for further study. 
 Here we review the features of successful expression\, purification and ch
 aracterization strategies that have underpinned these successes and that w
 ill drive further breakthroughs in the field. Summarizing\nthe production 
 processes which has resulted in high resolution aquaporin structures revea
 ls that Escherichia coli is a suitable host for prokaryotic isoforms\, whi
 le Pichia pastoris is the most\ncommonly used recombinant host for eukaryo
 tic variants. Generally\, a two-step purification procedure is applied aft
 er solubilization in glucopyranosides and most structures are determined b
 y X-ray following crystallization.\n\nhttps://lindico453.srv.lu.se/event/2
 19/contributions/1130/
LOCATION:
URL:https://lindico453.srv.lu.se/event/219/contributions/1130/
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BEGIN:VEVENT
SUMMARY:Contr. talk - The baculovirus/insect cells system
DTSTART;VALUE=DATE-TIME:20210525T111500Z
DTEND;VALUE=DATE-TIME:20210525T113500Z
DTSTAMP;VALUE=DATE-TIME:20260722T083934Z
UID:indico-contribution-182-1129@lindico453.srv.lu.se
DESCRIPTION:Speakers: Jan H Driller (Aarhus University)\nMammalian membran
 e proteins are notoriously difficult to express. In contrast to bacteria o
 r yeast\, the baculovirus/insect cells system provides a good alternative 
 to express these proteins in higher eukaryotes. Insect cells provide post-
 translational modifications\, such as disulfide bonds or glycosylation\, a
 s well as a more akin membrane lipid composition compared to bacterial or 
 yeast expression systems. Insect cells grow to high cell densities and usi
 ng the baculovirus system even multi-protein complexes can be co-expressed
 .\n\nhttps://lindico453.srv.lu.se/event/219/contributions/1129/
LOCATION:
URL:https://lindico453.srv.lu.se/event/219/contributions/1129/
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BEGIN:VEVENT
SUMMARY:Keynote talk - Recombinant membrane protein production in microbia
 l hosts
DTSTART;VALUE=DATE-TIME:20210525T103500Z
DTEND;VALUE=DATE-TIME:20210525T111500Z
DTSTAMP;VALUE=DATE-TIME:20260722T083934Z
UID:indico-contribution-182-1128@lindico453.srv.lu.se
DESCRIPTION:Speakers: Roslyn Bill (Aston University\, UK)\nDespite many hi
 gh-profile successes\, recombinant membrane protein production remains a t
 echnical challenge\; it is still the case that many fewer membrane protein
  structures have\nbeen published than those of soluble proteins. However\,
  progress is being made because empirical methods have been developed to p
 roduce the required quantity and quality of\nthese challenging targets. Mi
 crobial expression systems are a key source of recombinant prokaryotic and
  eukaryotic membrane proteins for structural studies. A combination of rat
 ional construct design and host cell choice can dramatically improve membr
 ane protein yields suitable for structural and functional characterization
 . In addition to traditional detergents\, polymer-based systems are availa
 ble for solubilization and biophysical characterization of these proteins\
 , with polymers providing opportunities to investigate protein-lipid inter
 actions.\n\nhttps://lindico453.srv.lu.se/event/219/contributions/1128/
LOCATION:
URL:https://lindico453.srv.lu.se/event/219/contributions/1128/
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