Research Briefing |
Featured
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Mirror-image trypsin digestion and sequencing of D-proteins
The lack of effective methods for mirror-image (d-) protein sequencing hampers the development of mirror-image biology systems and related applications. Now, total chemical synthesis of mirror-image trypsin enables the sequencing of long d-peptides and d-proteins, which may facilitate applications of d-peptides and d-proteins as potential therapeutic and informational tools.
- Guanwei Zhang
- & Ting F. Zhu
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Article |
Pervasive transcriptome interactions of protein-targeted drugs
Now a reactivity-based RNA profiling strategy can measure the global off-target transcriptome interactions of small-molecule drugs at single-nucleotide resolution. Using this approach, three FDA-approved drugs were evaluated, uncovering pervasive drug–RNA interactions and interactions that perturb RNA functions in cells.
- Linglan Fang
- , Willem A. Velema
- & Eric T. Kool
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News & Views |
Handling a protein with a nanopore machine
A protein–nanopore machine that can unfold, thread and degrade a protein has now been developed. Fabricated in a bottom-up fashion, the nanopore machine is assembled from three proteins and provides an important step towards deciphering the sequence of single proteins via nanopores.
- Yi-Lun Ying
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Article |
Bottom-up fabrication of a proteasome–nanopore that unravels and processes single proteins
An integrated multiprotein nanopore has been fabricated using components from all three domains of life. This molecular machine opens the door to two approaches in single-molecule protein analysis, in which selected substrate proteins are unfolded, fed to into the proteasomal chamber and then processed either as fragmented peptides or intact polypeptides.
- Shengli Zhang
- , Gang Huang
- & Giovanni Maglia
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Article |
An integrated native mass spectrometry and top-down proteomics method that connects sequence to structure and function of macromolecular complexes
An integrated native mass spectrometry and top-down proteomics method using Fourier transform ion cyclotron resonance has been developed for the characterization of macromolecular protein complexes. This approach directly yields primary to quaternary structural information in a single native top-down experiment.
- Huilin Li
- , Hong Hanh Nguyen
- & Joseph A. Loo