Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 107, Issue 18, Pages 8165-8170Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0914229107
Keywords
alpha-hemolysin; single molecule; stochastic sensing; structure; unnatural amino acid
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Funding
- Royal Society Wolfson Research Merit Award
- Medical Research Council
- National Institutes of Health
- Howard Hughes Medical Institute
- Medical Research Council [G0300122] Funding Source: researchfish
- MRC [G0300122] Funding Source: UKRI
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Engineered protein pores have several potential applications in biotechnology: as sensor elements in stochastic detection and ultrarapid DNA sequencing, as nanoreactors to observe single-molecule chemistry, and in the construction of nano- and micro-devices. One important class of pores contains molecular adapters, which provide internal binding sites for small molecules. Mutants of the alpha-hemolysin (alpha HL) pore that bind the adapter beta-cyclodextrin (beta CD) similar to 10(4) times more tightly than the wild type have been obtained. We now use single-channel electrical recording, protein engineering including unnatural amino acid mutagenesis, and high-resolution x-ray crystallography to provide definitive structural information on these engineered protein nanopores in unparalleled detail.
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