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

A thermoresistant mutant of ribonuclease T1 having three disulfide bonds.

Protein engineering - 1 Apr 1990

Nishikawa S, Adiwinata J, Morioka H, Fujimura T, Tanaka T, Uesugi S, Hakoshima T, Tomita K, Nakagawa S, Ikehara M

Abstract excerpt

Molecular-dynamic calculations predict that, if Tyr24 and Asn84 are each replaced by a Cys residue, it should be possible to form a third disulfide bond in ribonuclease T1 (RNase T1) between these residues, with only minimal conformational changes at the catalytic site. The gene encoding such a mutant variant of RNase T1 (Tyr24----Cys24, Asn84----Cys84) was constructed by the cassette mutagenesis method using a...

Read the complete abstract on PubMed

Topics

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

Share to Base Sequence
Share to Circular Dichroism
Share to Electrophoresis, Polyacrylamide Gel

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

Share to Gene Expression Regulation

Share to Models, Molecular

Share to Molecular Sequence Data

Share to Mutation

Share to Temperature

Source

Identifiers

PMID: 2349214
DOI: 10.1093/protein/3.5.443

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

A thermoresistant mutant of ribonuclease T1 having three disulfide bonds.PMID 2349214Read ↗

Structures of randomly generated mutants of T4 lysozyme show that protein stability can be enhanced by relaxation of strain and by improved hydrogen bonding via bound solvent.Semantic proximity Read ↗

Amino acids conserved at the C-terminal half of the ribonuclease T2 family contribute to protein stability of the enzymes.Semantic proximity Read ↗

Lessons from the lysozyme of phage T4.Semantic proximity Read ↗

RNase T1 variant RV cleaves single-stranded RNA after purines due to specific recognition by the Asn46 side chain amide.Semantic proximity Read ↗

Manipulation of the conformation and enzymatic properties of T1 lipase by site-directed mutagenesis of the protein core.Semantic proximity Read ↗

Thermal unfolding of chitosanase from Streptomyces sp. N174: role of tryptophan residues in the protein structure stabilization.Semantic proximity Read ↗

Significant stabilization of ribonuclease A by additive effects.Semantic proximity Read ↗

Expression of wild-type and mutant bovine pancreatic ribonuclease A in Escherichia coli.Semantic proximity Read ↗

Contribution of histidine residues to the conformational stability of ribonuclease T1 and mutant Glu-58----Ala.Semantic proximity Read ↗

Crystal structure of the Tyr45Trp mutant of ribonuclease T1 in a complex with 2'-adenylic acid.Semantic proximity Read ↗

Histidine-40 of ribonuclease T1 acts as base catalyst when the true catalytic base, glutamic acid-58, is replaced by alanine.Semantic proximity Read ↗

Remarkable stabilization of a psychrotrophic RNase HI by a combination of thermostabilizing mutations identified by the suppressor mutation method.Semantic proximity Read ↗

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