Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Steric and thermodynamic limits of design for the incorporation of large unnatural amino acids in aminoacyl-tRNA synthetase enzymes.

Proteins - 1 Jun 2010

Armen Roger S, Schiller Stefan M, Brooks Charles L

Abstract excerpt

Orthogonal aminoacyl-tRNA synthetase/tRNA pairs from archaea have been evolved to facilitate site specific in vivo incorporation of unnatural amino acids into proteins in Escherichia coli. Using this approach, unnatural amino acids have been successfully incorporated with high translational effic...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acids
Share to Amino Acyl-tRNA Synthetases
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Enzyme Stability

Share to Hydrogen Bonding

Share to Ligands

Share to Protein Structure, Secondary

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 20310065
DOI: 10.1002/prot.22706
PMCID: PMC4442682

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20310065-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Steric and thermodynamic limits of design for the incorporation of large unnatural amino acids in aminoacyl-tRNA synthetase enzymes.PMID 20310065Read ↗

Rational design of aminoacyl-tRNA synthetase specific for p-acetyl-L-phenylalanine.Semantic proximity Read ↗

Stereochemical basis for engineered pyrrolysyl-tRNA synthetase and the efficient in vivo incorporation of structurally divergent non-native amino acids.Semantic proximity Read ↗

A rationally designed pyrrolysyl-tRNA synthetase mutant with a broad substrate spectrum.Semantic proximity Read ↗

Transition State-Based Computational Enzyme Design.Semantic proximity Read ↗

An Orthogonal Tyrosyl-tRNA Synthetase/tRNA Pair from a Thermophilic Bacterium for an Expanded Eukaryotic Genetic Code.Semantic proximity Read ↗

Directed evolution of aminoacyl-tRNA synthetases through in vivo hypermutation.Semantic proximity Read ↗

A chemical toolkit for proteins--an expanded genetic code.Semantic proximity Read ↗

Adaptive landscape flattening allows the design of both enzyme: Substrate binding and catalytic power.Semantic proximity Read ↗

Elongation factor Tu mutants expand amino acid tolerance of protein biosynthesis system.Semantic proximity Read ↗

Thermophilic Pyrrolysyl-tRNA Synthetase Mutants for Enhanced Mammalian Genetic Code Expansion.Semantic proximity Read ↗

Making proteins with unnatural amino acids: the first engineered aminoacyl-tRNA synthetase revisited.Semantic proximity Read ↗

A Designed, Highly Efficient Pyrrolysyl-tRNA Synthetase Mutant Binds o-Chlorophenylalanine Using Two Halogen Bonds.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.