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

Aromatic rescue of glycine in beta sheets.

Folding & design - 1 Jan 1998

Merkel J S, Regan L

Abstract excerpt

BACKGROUND: Glycine is an intrinsically destabilizing residue in beta sheets. In natural proteins, however, this destabilization can be 'rescued' by specific cross-strand pairing with aromatic residues. Here, we present an experimental study of this effect. RESULTS: Protein variants containing glycine and aromatic residues positioned across beta strands in both antiparallel and parallel orientations were studied....

Read the complete abstract on PubMed

Topics

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

Share to Protein Folding
Share to Proteins
Share to Thermodynamics

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

Share to Mutation

Share to Glycine

Share to Models, Molecular

Source

Identifiers

PMID: 9889161
DOI: 10.1016/s1359-0278(98)00062-5

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

Aromatic rescue of glycine in beta sheets.PMID 9889161Read ↗

An energetically beneficial leader-linker interaction abolishes ligand-binding cooperativity in glycine riboswitches.Semantic proximity Read ↗

Aromatic cross-strand ladders control the structure and stability of beta-rich peptide self-assembly mimics.Semantic proximity Read ↗

Modulation of quaternary structure and enhancement of ligand binding by the K-turn of tandem glycine riboswitches.Semantic proximity Read ↗

Glycosylation of the enhanced aromatic sequon is similarly stabilizing in three distinct reverse turn contexts.Semantic proximity Read ↗

Transmembrane glycine zippers: physiological and pathological roles in membrane proteins.Semantic proximity Read ↗

Ligand binding by the tandem glycine riboswitch depends on aptamer dimerization but not double ligand occupancy.Semantic proximity Read ↗

Glycine at Position 93 in SOD1: Mutation-Sensitivity Landscape and Context-Dependent Folding Requirements.Semantic proximity Read ↗

A glycine zipper motif mediates the formation of toxic β-amyloid oligomers in vitro and in vivoSemantic proximity Read ↗

Modulating protein folding rates in vivo and in vitro by side-chain interactions between the parallel beta strands of green fluorescent protein.Semantic proximity Read ↗

Backbone double-mutant cycle analysis quantifies hydrogen-bond energies in proteins.Semantic proximity Read ↗

Aggregation gatekeeper and controlled assembly of Trpzip β-hairpins.Semantic proximity Read ↗

Engineering protein sequence composition for folding robustness renders efficient noncanonical amino acid incorporations.Semantic proximity Read ↗

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