John William Young

ORCID: 0000-0003-3541-509X
Publications
Citations
Views
---
Saved
---
About
Contact & Profiles
Research Areas
  • RNA and protein synthesis mechanisms
  • Lipid Membrane Structure and Behavior
  • Bacterial Genetics and Biotechnology
  • Protein Structure and Dynamics
  • Advanced Proteomics Techniques and Applications
  • Antioxidant Activity and Oxidative Stress
  • Bacteriophages and microbial interactions
  • Edible Oils Quality and Analysis
  • Photosynthetic Processes and Mechanisms
  • Advanced biosensing and bioanalysis techniques
  • Fatty Acid Research and Health
  • Cellular transport and secretion
  • Endoplasmic Reticulum Stress and Disease
  • Biotin and Related Studies
  • Antimicrobial Peptides and Activities
  • Advanced Fluorescence Microscopy Techniques
  • Machine Learning in Bioinformatics
  • Monoclonal and Polyclonal Antibodies Research
  • Clinical Nutrition and Gastroenterology
  • Mass Spectrometry Techniques and Applications
  • Neurobiology of Language and Bilingualism
  • Traumatic Brain Injury and Neurovascular Disturbances
  • Genomics and Phylogenetic Studies
  • Glycosylation and Glycoproteins Research
  • Escherichia coli research studies

University of British Columbia
2013-2025

University of Oxford
2023-2025

Austin Hospital
2009

Membrane proteins are difficult to work with due their insolubility in aqueous solution and quite often poor stability detergent micelles. Here, we present the peptidisc for facile capture into water-soluble particles. Unlike nanodisc, which requires scaffold of different lengths precise amounts matching lipids, reconstitution solubilized only a short amphipathic bi-helical peptide (NSPr) no extra lipids. Multiple copies wrap around shield membrane-exposed part target protein. We demonstrate...

10.7554/elife.34085 article EN cc-by eLife 2018-08-15

Protein-correlation-profiling (PCP), in combination with quantitative proteomics, has emerged as a high-throughput method for the rapid identification of dynamic protein complexes native conditions. While PCP been successfully applied to soluble proteomes, characterization membrane interactome lagged, partly due necessary use detergents maintain solubility. Here, we apply peptidisc, ‘one-size fits all’ mimetic, capture Escherichia coli cell envelope proteome and its high-resolution...

10.7554/elife.46615 article EN cc-by eLife 2019-07-31

Membrane proteins play critical roles at the cell surface, and their misfunction is a hallmark of many human diseases. A precise evaluation plasma membrane proteome is, therefore, essential for biology discovering novel biomarkers therapeutic targets. However, low abundance this relative to soluble makes it difficult characterize, even with most advanced proteomics technologies. Here, we apply peptidisc mimetic purify proteome. Using HeLa line as reference, capture 500 different integral...

10.1016/j.mcpro.2023.100588 article EN cc-by Molecular & Cellular Proteomics 2023-06-08

Membrane proteins perform numerous critical functions in the cell, making many of them primary drug targets. However, their preference for a lipid environment makes challenging to study using established solution-based methods. Here, we show that peptidiscs, recently developed membrane mimetic, provide an ideal platform and interactions with mass photometry (MP) detergent-free conditions. The resolution protein complexes is similar achievable soluble owing low carrier heterogeneity. Using...

10.1016/j.isci.2024.108785 article EN cc-by iScience 2024-01-04

The peptidisc membrane mimetic enables global reconstitution of the bacterial proteome into water-soluble detergent-free particles, termed libraries. We present here a method that combines libraries and chromosomal-level gene tagging technology with affinity purification mass spectrometry (AP/MS) to stabilize identify fragile protein complexes exist at native expression levels. This circumvents common artifacts caused by bait overproduction complex dissociation due lengthy exposure...

10.1021/acs.jproteome.2c00129 article EN Journal of Proteome Research 2022-05-26

YidC, a prominent member of the Oxa1 superfamily, is essential for biogenesis bacterial inner membrane, significantly influencing its protein composition and lipid organization. It interacts with Sec translocon, aiding proper folding multi-pass membrane proteins. also functions independently, serving as an insertase scramblase, augmenting insertion smaller proteins while contributing to organization bilayer. Despite wealth structural biochemical data available, how YidC operates remains...

10.1016/j.jbc.2025.108395 article EN cc-by-nc-nd Journal of Biological Chemistry 2025-03-01

Characterization of the integral membrane proteome by mass spectrometry (MS) remains challenging due its high complexity and inherent insolubility. In a typical experiment, cellular membranes are isolated, proteins solubilized fractionated, detergent micelles removed before MS analysis. Detergents not compatible with spectrometry, however, their removal from biological samples often results in reduced protein identification. As an alternative to detergents, we recently developed peptidisc...

10.1021/acs.jproteome.0c00022 article EN Journal of Proteome Research 2020-05-04

The outer membrane of Gram-negative bacteria plays a critical role in protecting the cell against external stressors, including antibiotics, and therefore is prime target for antimicrobial discovery. To facilitate discovery efforts, precise knowledge proteome, possible variations during pathogenesis, important. Characterization bacterial remain challenging, however, low throughput, due to high hydrophobicity relatively abundance this compartment. Here we adapt our peptidisc-based method...

10.1021/acs.jproteome.2c00560 article EN Journal of Proteome Research 2022-12-14

<p>The tocopherol (Toc) isoforms in 14 edible oils were determined and related to lipid oxidation of the oils. Oxidative stability vegetable was assessed using Rancimat analysis. The these at specific phases by measuring primary products generated during propagation phase (conjugated dienes trienes), peroxides (iodometric assay), together with secondary (TBARS assay). naturally occurring α-Toc level correlated (R = 0.696; P < 0.05) conjugated diene oils, indicating a potential...

10.32920/26093596 preprint EN 2024-06-27

<p>The tocopherol (Toc) isoforms in 14 edible oils were determined and related to lipid oxidation of the oils. Oxidative stability vegetable was assessed using Rancimat analysis. The these at specific phases by measuring primary products generated during propagation phase (conjugated dienes trienes), peroxides (iodometric assay), together with secondary (TBARS assay). naturally occurring α-Toc level correlated (R = 0.696; P < 0.05) conjugated diene oils, indicating a potential...

10.32920/26093596.v1 preprint EN 2024-06-27

YidC, a prominent member of the Oxa1 superfamily, is essential for biogenesis bacterial inner membrane, significantly influencing its protein composition and lipid organization. It interacts with Sec translocon, aiding proper folding multi-pass membrane proteins. also functions independently, serving as an insertase scramblase, augmenting insertion smaller proteins while contributing to organization bilayer. Despite wealth structural biochemical data available, how YidC operates remains...

10.1101/2024.12.13.628402 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2024-12-14

Many soluble proteins interact with membranes to perform important biological functions, including signal transduction, regulation, transport, trafficking, and biogenesis. Despite their importance, these protein–membrane interactions are difficult characterize due often-transient nature as well phospholipids' poor solubility in aqueous solution. Here, we employ nanodiscs—small, water-soluble patches of a lipid bilayer encircled amphipathic scaffold proteins—along quantitative proteomics...

10.1021/acs.jproteome.1c00503 article EN Journal of Proteome Research 2021-09-14

ABSTRACT Protein-correlation-profiling (PCP), in combination with quantitative proteomics, has emerged as a high-throughput method for the rapid identification of dynamic protein complexes native conditions. While PCP been successfully applied to soluble proteomes, characterization membrane interactome lagged, partly due necessary use detergents maintain solubility. Here, we apply peptidisc, ‘one-size fits all’ mimetic, capture Escherichia coli cell envelope proteome and its high-resolution...

10.1101/705418 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2019-07-17

ABSTRACT Membrane proteins perform a variety of critical functions in the cell, making many them primary drug targets. At same time, their preference for lipid environment makes challenging to study using established solution-based methods. Here, we show that peptidiscs, recently developed membrane mimetic, provide an ideal platform and interactions with mass photometry (MP) detergent-free conditions. The resolution protein complexes is similar achievable soluble owing low carrier...

10.1101/2023.06.01.543083 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2023-06-02

ABSTRACT The peptidisc membrane mimetic enables global reconstitution of the bacterial proteome into water-soluble detergent-free particles, termed libraries. We present here a method that combines libraries and chromosomal-level gene tagging technology with affinity purification mass spectrometry (AP/MS) to stabilize identify fragile protein complexes exist at native expression levels. This circumvents common artifacts caused by bait overproduction complex dissociation due lengthy exposure...

10.1101/2022.03.03.482899 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2022-03-03

ABSTRACT Many soluble proteins interact with membranes to perform important biological functions, including signal transduction, regulation, transport, trafficking and biogenesis. Despite their importance, these protein-membrane interactions are difficult characterize due often-transient nature as well phospholipids’ poor solubility in aqueous solution. Here, we employ nanodiscs – small, water-soluble patches of lipid bilayer encircled amphipathic scaffold along quantitative proteomics...

10.1101/2021.06.18.448950 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2021-06-18
Coming Soon ...