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

Silent mutations affect in vivo protein folding in Escherichia coli.

Biochemical and biophysical research communications - 26 Apr 2002

Cortazzo Patricia, Cerveñansky Carlos, Marín Mónica, Reiss Claude, Ehrlich Ricardo, Deana Atilio

Abstract excerpt

As an approach to investigate the molecular mechanism of in vivo protein folding and the role of translation kinetics on specific folding pathways, we made codon substitutions in the EgFABP1 (Echinococcus granulosus fatty acid binding protein1) gene that replaced five minor codons with their synonymous major ones. The altered region corresponds to a turn between two short alpha helices. One of the silent...

Read the complete abstract on PubMed

Topics

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

Share to Carrier Proteins
Share to Codon
Share to Fatty Acid-Binding Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Fish Proteins

Share to Oligodeoxyribonucleotides

Share to Peptide Fragments

Share to Protein Folding

Share to Protein Structure, Secondary

Source

Identifiers

PMID: 12054634
DOI: 10.1016/S0006-291X(02)00226-7

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Silent mutations affect in vivo protein folding in Escherichia coli.PMID 12054634Read ↗

Early folding events protect aggregation-prone regions of a β-rich protein.Semantic proximity Read ↗

Transient folding intermediates characterized by protein engineering.Semantic proximity Read ↗

Low-Level Expression of a Folding-Incompetent Protein in Escherichia coli: Search for the Molecular Determinants of Protein Aggregation In VivoSemantic proximity Read ↗

Green fluorescent protein variants fold differentially in prokaryotic and eukaryotic cells.Semantic proximity Read ↗

Comparison between medium-chain acyl-CoA dehydrogenase mutant proteins overexpressed in bacterial and mammalian cells.Semantic proximity Read ↗

Stabilisation of alpha-helices by site-directed mutagenesis reveals the importance of secondary structure in the transition state for acylphosphatase folding.Semantic proximity Read ↗

Slowing bacterial translation speed enhances eukaryotic protein folding efficiency.Semantic proximity Read ↗

Mutations of key hydrophobic surface residues of 11 beta-hydroxysteroid dehydrogenase type 1 increase solubility and monodispersity in a bacterial expression system.Semantic proximity Read ↗

Folding and aggregation are selectively influenced by the conformational preferences of the alpha-helices of muscle acylphosphatase.Semantic proximity Read ↗

Intestinal fatty acid-binding protein: the structure and stability of a helix-less variant.Semantic proximity Read ↗

Errors of heterologous protein expression.Semantic proximity Read ↗

Directed evolution study unveiling key sequence factors that affect translation efficiency in Escherichia coli.Semantic proximity Read ↗

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