Characterization of Guest DNA Transport and Adsorption within Host Porous Protein Crystals.
Ontology highlight
ABSTRACT: Nucleic acid transport through protein-based pores is a well-characterized phenomenon due in part to advancements in nanopore sequencing. A less studied area is nucleic acid transport through extended protein-based channels, where the additional surface area and increased contact time allow for the study of prolonged binding interactions. Porous protein crystals composed of "CJ", a putative polyisoprenoid-binding protein from Campylobacter jejuni, represent a favorable, highly ordered material for studying DNA transport and binding/unbinding along protein-based channels. These crystals adopt a hexagonal prism habit and contain a densely packed hexagonal array of 13 nm diameter axial nanopores that run from the top to the bottom of the crystal. After cross-linking, the crystals are e
SUBMITTER: Chen S
PROVIDER: S-EPMC11657527 | biostudies-literature | 2024 Dec
REPOSITORIES: biostudies-literature
ACCESS DATA