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

The length of a single turn controls the overall folding rate of "three-fingered" snake toxins.

Biochemistry - 17 Nov 1998

Ruoppolo M, Moutiez M, Mazzeo M F, Pucci P, Ménez A, Marino G, Quéméneur E

Abstract excerpt

Snake curaremimetic toxins are short all-beta proteins, containing several disulfide bonds which largely contribute to their stability. The four disulfides present in snake toxins make a "disulfide beta-cross"-fold that was suggested to be a good protein folding template. Previous studies on the refolding of snake toxins (Ménez, A. et al. (1980) Biochemistry 19, 4166-4172) showed that this set of natural...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Amino Acid Substitution
Share to Mass Spectrometry

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

Share to Molecular Sequence Data

Share to Mutation

Share to Peptide Mapping

Share to Protein Folding

Share to Protein Structure, Secondary

Source

Identifiers

PMID: 9819199
DOI: 10.1021/bi981492j

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

The length of a single turn controls the overall folding rate of "three-fingered" snake toxins.PMID 9819199Read ↗

Three-fingered RAVERs: Rapid Accumulation of Variations in Exposed Residues of snake venom toxins.Semantic proximity Read ↗

Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure.Semantic proximity Read ↗

Impact of an easily reducible disulfide bond on the oxidative folding rate of multi-disulfide-containing proteins.Semantic proximity Read ↗

Molecular evolution and diversification of snake toxin genes, revealed by analysis of intron sequences.Semantic proximity Read ↗

Pore formation by equinatoxin, a eukaryotic pore-forming toxin, requires a flexible N-terminal region and a stable beta-sandwich.Semantic proximity Read ↗

The origami of thioredoxin-like folds.Semantic proximity Read ↗

Bacterial expression, NMR, and electrophysiology analysis of chimeric short/long-chain alpha-neurotoxins acting on neuronal nicotinic receptors.Semantic proximity Read ↗

Regeneration of three-disulfide mutants of bovine pancreatic ribonuclease A missing the 65-72 disulfide bond: characterization of a minor folding pathway of ribonuclease A and kinetic roles of Cys65 and Cys72.Semantic proximity Read ↗

Apparent two-state tendamistat folding is a sequential process along a defined route.Semantic proximity Read ↗

Maurotoxin versus Pi1/HsTx1 scorpion toxins. Toward new insights in the understanding of their distinct disulfide bridge patterns.Semantic proximity Read ↗

Disulfide bridge reorganization induced by proline mutations in maurotoxin.Semantic proximity Read ↗

Disulfide bonds of phospholipase A2 from bee venom yield discrete contributions to its conformational stability.Semantic proximity Read ↗

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