ArticleThe journal of physical chemistry. B2025
Effects of Nanopore Confinement on the Conformational, Dynamical, and Self-Assembly Properties of an FG-Repeat Peptide.
Article in The journal of physical chemistry. B, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Karyopherins remodel the dynamic organization of the nuclear pore complex transport barrier.Nature cell biology · 2025Article
- Integrative mapping reveals molecular features underlying the mechanism of nucleocytoplasmic transport.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
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Abstract
The central channels of nuclear pore complexes (NPCs) in eukaryotic cells are filled with protein chains whose sequences contain characteristic phenylalanine-glycine motifs. Properties of these nanopore-confined FG-repeat sequences are of central importance to NPC function. Here, we demonstrate an approach to nuclear magnetic resonance (NMR) studies of FG-repeat sequences (or other polypeptides) that are tethered within pores with diameters similar to those of NPC channels. By attaching alkyl phosphonate groups to the N-terminus of a 30-residue peptide that contains four FG repeats, called FG30, we tether FG30 chains to walls of 20 nm-diameter pores in anodic aluminum oxide (AAO) wafers through phosphonate-surface bonds. Quantitative
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