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Tycko - 2026

Mentor: Robert Tycko, Ph.D. | robertty@mail.nih.gov
Lab
Solid State NMR and Biomolecular Physics Section, Laboratory of Chemical Physics, NIDDK

Properties of nanoconfined peptides and proteins in anodic aluminum oxide nanopores

Our lab uses a wide variety of biophysical and structural techniques to investigate essential properties of biopolymers and macromolecular assemblies with important roles in biology and human diseases. Recent work includes: (i) structural studies of amyloid fibrils associated with neurodegenerative diseases, based on nuclear magnetic resonance (NMR) and cryogenic electron microscopy (cryoEM) methods; (ii) studies of molecular mechanisms of protein folding and self-assembly, based on time-resolved NMR techniques developed in our lab; (iii) micron-scale magnetic resonance imaging (MRI), based on novel low-temperature NMR technology.

One of our latest projects is to study the conformations, motions, and interactions of intrinsically disordered proteins and peptides within pores with 20-80 nm diameters, motivated by questions regarding the mechanism of selective macromolecular transport through the nuclear pore channels of eukaryotic cells. These experiments depend on covalent attachment of proteins and peptides to nanopore walls in anodic aluminum oxide wafers, which we accomplish with phosphonate-aluminum oxide chemistry. Initial results from NMR and confocal fluorescence microscopy show that very high intrapore peptide densities can be achieved (~300 mg/ml) and that nanopore confinement dramatically alters dynamics and aggregation propensities (see https://pubs.acs.org/doi/10.1021/acs.jpcb.5c07676). Investigations of the dependence of protein dynamics on amino acid sequence, sequence length, density, temperature, interactions nuclear transport receptors, etc. are planned.

The BESIP student will participate in aspects of this multidisciplinary research that align most closely with the student’s interests and background, possibly including optimization of sample preparations, fabrication of novel equipment for measurements of intrapore diffusion rates, NMR measurements of protein dynamics, fluorescence microscopy measurements of protein density distributions, etc.