2021
DOI: 10.1039/d0sc06106a
|View full text |Cite
|
Sign up to set email alerts
|

Snapshotting the transient conformations and tracing the multiple pathways of single peptide folding using a solid-state nanopore

Abstract: A solid-state nanopore based method is described for resolving protein-folding-related problems via snapshotting the folding intermediates and characterizing the kinetics of a single peptide.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

0
34
0

Year Published

2021
2021
2024
2024

Publication Types

Select...
8
1

Relationship

3
6

Authors

Journals

citations
Cited by 43 publications
(34 citation statements)
references
References 60 publications
0
34
0
Order By: Relevance
“…However, whether this will affect the manipulation effectiveness still remains a mystery. In real experiments, strong binding between streptavidin (gold) and biotin (thiol) [ 41 ] could be used to attach biotinylated DNA to streptavidin‐coated nanoparticles for assembling the multi‐leg nanorobot, the substrate could be fabricated by the existing MEMS and CMOS technology, and the surface charge density of each nanopore could be changed by tuning the gate voltage on the embedded metal electrodes in the membrane. Anyway, the experimental setup of the encoding manipulation system is possible in the near future though some challenges still remain to be solved firstly, which is also the future study researchers may focus on.…”
Section: Discussionmentioning
confidence: 99%
“…However, whether this will affect the manipulation effectiveness still remains a mystery. In real experiments, strong binding between streptavidin (gold) and biotin (thiol) [ 41 ] could be used to attach biotinylated DNA to streptavidin‐coated nanoparticles for assembling the multi‐leg nanorobot, the substrate could be fabricated by the existing MEMS and CMOS technology, and the surface charge density of each nanopore could be changed by tuning the gate voltage on the embedded metal electrodes in the membrane. Anyway, the experimental setup of the encoding manipulation system is possible in the near future though some challenges still remain to be solved firstly, which is also the future study researchers may focus on.…”
Section: Discussionmentioning
confidence: 99%
“…In one example, a protein stopper was introduced to immobilize a biotinylated peptide inside a nanopore, allowing the measurement of multiple conformational transition pathways (Fig. 2e) 83 . In another recent report, a DNA lid was added to one side of a lipid-coated nanopore, and proteins were added to the opposite side (Fig.…”
Section: Characterization Of Single Proteins With Nanoporesmentioning
confidence: 99%
“…Examples include many aspects of the chemistry of thiols introduced as cysteine side chains 85 . Groups other than thiols can be examined after they have been introduced by site-directed chemical 83 . f, Immobilization of a protein (blue) inside a nanopore (grey) using a DNA origami sphere (red) as a NEOtrap (top left) 84 .…”
Section: Single-molecule Chemistry Within Biological Nanoporesmentioning
confidence: 99%
“…Specific recognition in the nanopore/nanochannel analyses can be achieved by surface modification of carefully selected probes with a strong interaction with targets. The captured targets tailor the properties of the nanopore/nanochannel, mainly including space charge and steric hindrance, and change the ionic signal. Up until now, it has realized the detection of multiple targets, covering ions, , small molecules, , polypeptides, , carbohydrates, nucleic acids, , proteins, and so on. The critical issue regarding specific recognition is to efficiently convert target characteristics into a detectable ionic signal in view of practical necessity for detecting trace targets in a complex matrix.…”
Section: Introductionmentioning
confidence: 99%