We are pleased to launch the 23/24 PPSG online seminar series with two fantastic talks.
The early career academics presenting in this seminar will be Dr Tom McAllister from Newcastle University (https://blogs.ncl.ac.uk/tommcallister/) and Dr Andrew Giltrap from the Rosalind Franklin Institute (https://www.rfi.ac.uk/people/dr-andrew-giltrap/).
Tom McAllister – Newcastle University
Title: Investigating Protein O-glycosylation
Abstract: Carbohydrates are involved in many important biological processes across all Kingdoms of life including how organisms recognise pathogens, how cancers can spread and the basis of the different A/B/O blood groups in humans. Glycosylation (modification with carbohydrates) is the most abundant and complex form of protein post-translational modification. Glycosylation of asparagine residues, N-glycans, is well established but other modifications such as the O-glycans formed by modifications of serine and threonine residues, are less well understood. Research in the McAllister group focuses on investigating the biosynthesis of O-glycans as well as methods to produce homogeneous O-glycopeptides/glycoproteins in order to decipher the role of specific glycans at specific sites.
Dr Andrew Giltrap – The Rosalind Franklin Institute
Title: Recent Advances in Radical Mediated Protein Editing
Abstract: After translation at the ribosome many proteins are adorned with so-called post translational modifications (PTMs) (e.g. methylation, glycosylation, phosphorylation etc) which impart specific structural and functional changes. A key challenge in developing chemical methods to produce modified proteins is the number of reactive functional groups present leading to chemo- and regio- selectivity issues, making the installation of truly native modifications extremely difficult. This has limited our ability to gain insights into how these modifications govern biological processes. One particularly promising approach to solve this problem is the use of radical chemistry. Here recent advances utilising this approach to site-specifically modify proteins, allowing for the installation of diverse functional groups, as well as approaches for in vivo protein editing will be detailed.
Seminars are hosted on the first Friday of each month. For details of future seminars in the series, please visit the UUÂãÁÄÖ±²¥ PPSG website
If you would like to present in future seminars, please contact one of the organisers.
Louis Luk: lukly@cardiff.ac.uk
Chris Coxon: chris.coxon@ed.ac.uk
Louise Walport: l.walport@imperial.ac.uk
The early career academics presenting in this seminar will be Dr Tom McAllister from Newcastle University (https://blogs.ncl.ac.uk/tommcallister/) and Dr Andrew Giltrap from the Rosalind Franklin Institute (https://www.rfi.ac.uk/people/dr-andrew-giltrap/).
Tom McAllister – Newcastle University
Title: Investigating Protein O-glycosylation
Abstract: Carbohydrates are involved in many important biological processes across all Kingdoms of life including how organisms recognise pathogens, how cancers can spread and the basis of the different A/B/O blood groups in humans. Glycosylation (modification with carbohydrates) is the most abundant and complex form of protein post-translational modification. Glycosylation of asparagine residues, N-glycans, is well established but other modifications such as the O-glycans formed by modifications of serine and threonine residues, are less well understood. Research in the McAllister group focuses on investigating the biosynthesis of O-glycans as well as methods to produce homogeneous O-glycopeptides/glycoproteins in order to decipher the role of specific glycans at specific sites.
Dr Andrew Giltrap – The Rosalind Franklin Institute
Title: Recent Advances in Radical Mediated Protein Editing
Abstract: After translation at the ribosome many proteins are adorned with so-called post translational modifications (PTMs) (e.g. methylation, glycosylation, phosphorylation etc) which impart specific structural and functional changes. A key challenge in developing chemical methods to produce modified proteins is the number of reactive functional groups present leading to chemo- and regio- selectivity issues, making the installation of truly native modifications extremely difficult. This has limited our ability to gain insights into how these modifications govern biological processes. One particularly promising approach to solve this problem is the use of radical chemistry. Here recent advances utilising this approach to site-specifically modify proteins, allowing for the installation of diverse functional groups, as well as approaches for in vivo protein editing will be detailed.
Seminars are hosted on the first Friday of each month. For details of future seminars in the series, please visit the UUÂãÁÄÖ±²¥ PPSG website
If you would like to present in future seminars, please contact one of the organisers.
Louis Luk: lukly@cardiff.ac.uk
Chris Coxon: chris.coxon@ed.ac.uk
Louise Walport: l.walport@imperial.ac.uk
