ORCID Profile
0000-0001-8003-8831
Current Organisations
University of Colorado at Boulder
,
Tulane University
,
Universität Wien
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Publisher: Springer Science and Business Media LLC
Date: 12-11-2022
DOI: 10.1038/S41467-022-34530-Z
Abstract: The importance of modified peptides and proteins for applications in drug discovery, and for illuminating biological processes at the molecular level, is fueling a demand for efficient methods that facilitate the precise modification of these biomolecules. Herein, we describe the development of a photocatalytic method for the rapid and efficient dimerization and site-specific functionalization of peptide and protein diselenides. This methodology, dubbed the photocatalytic diselenide contraction, involves irradiation at 450 nm in the presence of an iridium photocatalyst and a phosphine and results in rapid and clean conversion of diselenides to reductively stable selenoethers. A mechanism for this photocatalytic transformation is proposed, which is supported by photoluminescence spectroscopy and density functional theory calculations. The utility of the photocatalytic diselenide contraction transformation is highlighted through the dimerization of selenopeptides, and by the generation of two families of protein conjugates via the site-selective modification of calmodulin containing the 21 st amino acid selenocysteine, and the C-terminal modification of a ubiquitin diselenide.
Publisher: Royal Society of Chemistry (RSC)
Date: 2021
DOI: 10.1039/D0CB00175A
Abstract: Using protein semi-synthesis, segmentally isotope-labelled variants of nucleosome-binding protein HMGN1 were generated with site-specific posttranslational modifications to explore their structural and functional effects.
Publisher: Springer Science and Business Media LLC
Date: 22-05-2021
Publisher: American Chemical Society (ACS)
Date: 15-09-2020
DOI: 10.26434/CHEMRXIV.12950942.V1
Abstract: Interactions between histones, which package DNA in eukaryotes, and nuclear proteins such as the high mobility group nucleosome-binding protein HMGN1 are important for regulating access to DNA. HMGN1 is a highly charged and intrinsically disordered protein (IDP) that is modified at several sites by posttranslational modifications (PTMs) - acetylation, phosphorylation and ADP-ribosylation. These PTMs are thought to affect cellular localisation of HMGN1 and its ability to bind nucleosomes however, little is known about how these PTMs regulate the structure and function of HMGN1 at a molecular level. Here, we combine the chemical biology tools of protein semi-synthesis and site-specific modification to generate a series of unique HMGN1 variants bearing precise PTMs at their N- and C-termini with segmental isotope labelling for NMR spectroscopy. This study demonstrates the power of combining protein semi-synthesis for introduction of site-specific PTMs with segmental isotope labelling for structural biology, allowing us to understand the roles of PTMs with atomic precision, from both structural and functional perspectives.
Publisher: MDPI AG
Date: 22-09-2020
DOI: 10.3390/D12090363
Abstract: Microbial symbionts are gaining attention as crucial drivers of invasive species spread and dominance. To date, much research has quantified the net effects of plant–microbe interactions on the relative success of native and invasive species. However, little is known about how the structure (composition and ersity) of microbial symbionts can differ among native and invasive species, or vary across the invasive landscape. Here, we explore the structure of endosphere and soil fungal communities associated with a monoculture-forming widespread invader, Phragmites australis, and co-occurring native species. Using field survey data from marshes in coastal Louisiana, we tested three hypotheses: (1) Phragmites australis root and soil fungal communities differ from that of co-occurring natives, (2) Phragmites australis monocultures harbor distinct fungal communities at the expanding edge compared to the monodominant center, and (3) proximity to the P. australis invading front alters native root endosphere and soil fungal community structure. We found that P. australis cultivates root and soil fungal communities with higher richness, ersity, and pathogen abundances compared to native species. While P. australis was found to have higher endosphere pathogen abundances at its expanding edge compared to the monodominant center, we found no evidence of compositional changes or pathogen spillover in native species in close proximity to the invasion front. This work suggests that field measurements of fungal endosphere communities in native and invasive plants are useful to help understand (or rule out) mechanisms of invasion.
Publisher: Wiley
Date: 09-03-2021
Publisher: Royal Society of Chemistry (RSC)
Date: 2017
DOI: 10.1039/C7SC02719B
Abstract: Semisynthesis and characterization of homogeneously mono- and di-PEGylated full length PrP variants to study the impact of PEGylation (as N -glycan mimics) on protein folding and aggregation.
Publisher: Wiley
Date: 09-03-2022
Abstract: Herein, we describe the development and application of a novel expressed protein selenoester ligation (EPSL) methodology for the one-pot semi-synthesis of modified proteins. EPSL harnesses the rapid kinetics of ligation reactions between modified synthetic selenopeptides and protein aryl selenoesters (generated from expressed intein fusion precursors) followed by in situ chemoselective deselenization to afford target proteins at concentrations that preclude the use of traditional ligation methods. The utility of the EPSL technology is showcased through the efficient semi-synthesis of ubiquitinated polypeptides, lipidated analogues of the membrane-associated GTPase YPT6, and site-specifically phosphorylated variants of the oligomeric chaperone protein Hsp27 at high dilution.
Publisher: American Chemical Society (ACS)
Date: 15-09-2020
DOI: 10.26434/CHEMRXIV.12950942
Abstract: Interactions between histones, which package DNA in eukaryotes, and nuclear proteins such as the high mobility group nucleosome-binding protein HMGN1 are important for regulating access to DNA. HMGN1 is a highly charged and intrinsically disordered protein (IDP) that is modified at several sites by posttranslational modifications (PTMs) - acetylation, phosphorylation and ADP-ribosylation. These PTMs are thought to affect cellular localisation of HMGN1 and its ability to bind nucleosomes however, little is known about how these PTMs regulate the structure and function of HMGN1 at a molecular level. Here, we combine the chemical biology tools of protein semi-synthesis and site-specific modification to generate a series of unique HMGN1 variants bearing precise PTMs at their N- and C-termini with segmental isotope labelling for NMR spectroscopy. This study demonstrates the power of combining protein semi-synthesis for introduction of site-specific PTMs with segmental isotope labelling for structural biology, allowing us to understand the roles of PTMs with atomic precision, from both structural and functional perspectives. br
Location: United States of America
No related grants have been discovered for EMILY FARRER.