Nanopores as Single-Molecule Probes of Protein-Lipid Interactions
This grant explores using nanopores to study how proteins interact with lipid membranes, aiming to improve understanding of protein binding mechanisms.
This grant is no longer accepting proposals
NRC Research Associateship Programs has archived this opportunity.
Funder: NRC Research Associateship Programs
Due Dates: February 1, 2025 | May 1, 2025 | August 1, 2025 | November 1, 2025
Funding Amounts: Stipend approximately $82,764 per year plus $3,000 travel allowance; typical appointment duration 2 years.
Summary: Supports postdoctoral research at NIST to develop and apply nanopore-based single-molecule techniques for studying protein interactions with bilayer lipid membranes.
Key Information: Open to U.S. citizens with a doctoral degree earned within the last 5 years; requires contacting the research adviser prior to application; NIST participates in February and August review cycles.
Description
This fellowship opportunity at the National Institute of Standards and Technology (NIST) Center for Neutron Research focuses on advancing the understanding of protein-lipid interactions using nanopore technology. The research aims to elucidate the mechanisms by which proteins localize and bind to bilayer lipid membranes (BLMs), a fundamental but complex cellular process involving diverse binding mechanisms.
The bioreflectometry group at NIST collaborates with academic and government laboratories to develop advanced biochemical and biophysical methods, particularly those complementing neutron scattering studies of membrane-associated proteins. The research emphasizes:
- Development of new chemistries for measurement platforms.
- Protein synthesis and diagnostic techniques.
- Advanced data analysis and simulation methods.
- Instrument and sample environment development.
Two innovative techniques based on planar lipid bilayer architecture are central to this research:
- Bilayer overtone analysis: Measures electric field-induced compression of BLMs to detect membrane asymmetries caused by analyte binding.
- Reconstitution of biological nanopores into BLMs: Enables single-molecule probing of membrane binding properties, including binding energy.
These methods have been successfully applied to study mitochondrial regulators such as α-synuclein and dimeric tubulin, with plans to extend to other peripheral membrane proteins.
