Natalya A. Watson

ORCID: 0009-0009-5914-300X
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About
Contact & Profiles
Research Areas
  • Antimicrobial Peptides and Activities
  • Protein Structure and Dynamics
  • Receptor Mechanisms and Signaling
  • Biochemical and Structural Characterization
  • Nicotinic Acetylcholine Receptors Study
  • Protein purification and stability
  • Protein Hydrolysis and Bioactive Peptides
  • Probiotics and Fermented Foods

Concordia University
2022-2024

Concordia University
2024

Short, cysteine-rich peptides can exist in stable or metastable structural ensembles due to the number of possible patterns formation their disulfide bonds. One interesting subset this peptide group is conotoxins, which are produced by aquatic snails family Conidae. The μ antagonists and blockers voltage-gated sodium channel, a folding spectrum: on one end spectrum more hirudin-like folders, form bonds then reshuffle them, leading an ensemble kinetically trapped isomers, other BPTI-like...

10.1021/acs.jpcb.2c07124 article EN cc-by-nc-nd The Journal of Physical Chemistry B 2023-02-15

Antimicrobial peptides (AMPs) are of growing interest as potential candidates for antibiotics to which antimicrobial resistance increases slowly. In this article, we perform the first in silico study synthetic β sheet-forming AMP GL13K. Through atomistic simulations single and multipeptide systems under different charge conditions, able shine a light on short timescales early aggregation. We find that isolated peptide conformations primarily dictated by sequence rather than charge, whereas...

10.1101/2024.01.25.577308 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2024-01-28

Antimicrobial peptides (AMPs) are of growing interest as potential candidates that may offer more resilience against antimicrobial resistance than traditional antibiotic agents. In this article, we perform the first in silico study synthetic ß sheet-forming AMP GL13K. Through atomistic simulations single and multi-peptide systems under different conditions, able to shine a light on short timescales early aggregation. We find isolated peptide conformations primarily dictated by sequence...

10.1002/cbic.202400088 article EN cc-by-nc ChemBioChem 2024-04-04

Abstract Short, cysteine-rich peptides can exist in stable or metastable structural ensembles due to the number of possible patterns formation their disulfide bonds. One interesting subset this peptide group is coonotoxins, which are produced by aquatic snails family Conidae . The µ conotoxins, antagonists and blockers voltage-gated sodium channel, a folding spectrum: on one end spectrum more hirudin-like folders, form bonds then reshuffle them, leading an ensemble kinetically trapped...

10.1101/2022.10.07.511306 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2022-10-07
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