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

Effect of D57N mutation on membrane activity and molecular unfolding of cobra cardiotoxin.

Biophysical journal - 1 Nov 1998

Lo C C, Hsu J H, Sheu Y C, Chiang C M, Wu W g, Fann W, Tsao P H

Abstract excerpt

Cobra cardiotoxins (CTXs) are able to adopt a three-fingered beta-strand structure with continuous hydrophobic patch that is capable of interacting with zwitterionic phospholipid bilayer. In addition to the four disulfide bonds that form the rigid core of CTXs, Asp57 near the C-terminus interacts electrostatically with Lys2 near the N-terminus (Chiang et al. 1996. Biochemistry. 35:9177-9186). We indicate herein,...

Read the complete abstract on PubMed

Topics

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

Share to Circular Dichroism
Share to Fluorescent Dyes
Share to Models, Molecular

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

Share to Mutation

Share to Protein Folding

Share to Protein Structure, Secondary

Share to Spectrometry, Fluorescence

Share to Tryptophan

Source

Open in PubMed Open full text

Identifiers

PMID: 9788933
DOI: 10.1016/S0006-3495(98)77682-9
PMCID: PMC1299912

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

Effect of D57N mutation on membrane activity and molecular unfolding of cobra cardiotoxin.PMID 9788933Read ↗

Structural and denaturation studies of two mutants of a cold adapted superoxide dismutase point to the importance of electrostatic interactions in protein stability.Semantic proximity Read ↗

Interaction of Ca2(+)-activated K+ channels with refolded charybdotoxins mutated at a central interaction residue.Semantic proximity Read ↗

Effects of binding factors on structural elements in F-actin.Semantic proximity Read ↗

Production in Escherichia coli, folding, purification and characterization of notexin with wild type sequence and with N-terminal and catalytic site mutations.Semantic proximity Read ↗

Unusual effects of an engineered disulfide on global and local protein stability.Semantic proximity Read ↗

COOH-terminal truncations and site-directed mutations enhance thermostability and chaperone-like activity of porcine alphaB-crystallin.Semantic proximity Read ↗

Mutations on N-terminal region of Taiwan cobra phospholipase A(2) result in structurally distorted effects.Semantic proximity Read ↗

Structure of the Diphtheria Toxin at Acidic pH: Implications for the Conformational Switching of the Translocation Domain.Semantic proximity Read ↗

Contribution of tryptophan residues to the structural changes in perfringolysin O during interaction with liposomal membranes.Semantic proximity Read ↗

The effect of core destabilization on the mechanical resistance of I27.Semantic proximity Read ↗

Residue Phe266 in S5-S6 loop is not critical for Charybdotoxin binding to Ca2+-activated K+ (mSlo1) channels.Semantic proximity Read ↗

Human cytochrome C natural variants: Studying the membrane binding properties of G41S and Y48H by fluorescence energy transfer and molecular dynamics.Semantic proximity Read ↗

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