Article
|
Open Access
Featured
-
-
Article |
Engineering orthogonal signalling pathways reveals the sparse occupancy of sequence space
Engineered two-component signalling proteins in Escherichia coli have residue specificities different to their parent proteins and are orthogonal to all extant paralogues, demonstrating that sequence space is not densely occupied.
- Conor J. McClune
- , Aurora Alvarez-Buylla
- & Michael T. Laub
-
Letter |
The spatial architecture of protein function and adaptation
A high-throughput mutagenesis study in a PDZ domain shows that biochemical function and adaptation primarily originate from a collectively evolving amino acid network within the structure termed a protein sector.
- Richard N. McLaughlin Jr
- , Frank J. Poelwijk
- & Rama Ranganathan
-
Review Article |
Engineering the third wave of biocatalysis
Over the past ten years, protein engineering has established biocatalysis as a practical and environmentally friendly alternative to traditional forms of catalysis both in the laboratory and in industry.
- U. T. Bornscheuer
- , G. W. Huisman
- & K. Robins
-
News & Views |
Tighter ties that bind
A stepwise process of mutation and structural analysis has modulated a flexible binding interface of an immune-cell signalling protein, interleukin-2, and generated mutant proteins with enhanced anticancer activity. See Article p.529
- Eric T. Boder
-
News & Views |
Catalytic detoxification
Protein engineering of an enzyme that catalytically detoxifies organophosphate compounds in the body opens up fresh opportunities in the search for therapeutic protection against nerve agents used in chemical warfare.
- Frank M. Raushel
-
News & Views |
Longer-lived proteins
Short residence times in the bloodstream reduce the effectiveness of protein drugs. Application of an approach that combines protein and polymer engineering prolongs circulation time and increases drug uptake by tumours.
- Jeffrey A. Hubbell
-
Letter |
Encoding multiple unnatural amino acids via evolution of a quadruplet-decoding ribosome
Although new amino acids with desirable properties can be devised, only a few have been successfully introduced into proteins by the cellular machinery. Even then, only one type of unnatural amino acid can be added to a given protein. Here, a new system has been designed that could allow the incorporation of up to 200 novel amino acids. The system involves an orthogonal ribosome that uses quadruplet — rather than triplet — codons, as well as orthogonal tRNA synthetase–tRNA pairs.
- Heinz Neumann
- , Kaihang Wang
- & Jason W. Chin