Kavli Affiliate: Cees Dekker
| First 5 Authors: Sonja Schmid, Cees Dekker, , ,
| Summary:
Proteins are the active working horses in our body. These biomolecules
perform all vital cellular functions from DNA replication and general
biosynthesis to metabolic signaling and environmental sensing. While static 3D
structures are now readily available, observing the functional cycle of
proteins – involving conformational changes and interactions – remains very
challenging, e.g., due to ensemble averaging. However, time-resolved
information is crucial to gain a mechanistic understanding of protein function.
Single-molecule techniques such as FRET and force spectroscopies provide
answers but can be limited by the required labelling, a narrow time bandwidth,
and more. Here, we describe electrical nanopore detection as a tool for probing
protein dynamics. With a time bandwidth ranging from microseconds to hours, it
covers an exceptionally wide range of timescales that is very relevant for
protein function. First, we discuss the working principle of label-free
nanopore experiments, various pore designs, instrumentation, and the
characteristics of nanopore signals. In the second part, we review a few
nanopore experiments that solved research questions in protein science, and we
compare nanopores to other single-molecule techniques. We hope to make
electrical nanopore sensing more accessible to the biochemical community, and
to inspire new creative solutions to resolve a variety of protein dynamics –
one molecule at a time.
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