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 duplication of an eight-residue helical stretch in Staphylococcal nuclease is not helical: a model for evolutionary change.

Proteins - 15 Aug 2000

Nguyen D M, Gittis A G, Lattman E E

Abstract excerpt

A common method of evolutionary change is gene duplication, followed by other events that lead to new function, decoration of folds, oligomerization, or other changes. As part of a study on the potential for evolutionary change created by duplicated sequences, we have carried out a crystallographic study on a mutant of Staphylococcal nuclease in which residues 55-62 have been duplicated in a wild-type variant...

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 Computer Simulation
Share to Crystallography, X-Ray

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

Share to Gene Duplication

Share to Micrococcal Nuclease

Share to Oligopeptides

Share to Protein Structure, Secondary

Share to Repetitive Sequences, Amino Acid

Source

Identifiers

PMID: 10861938
DOI: 10.1002/1097-0134(20000815)40:3<465::aid-prot130>3.0.co;2-a

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 duplication of an eight-residue helical stretch in Staphylococcal nuclease is not helical: a model for evolutionary change.PMID 10861938Read ↗

Accommodation of single amino acid insertions by the native state of staphylococcal nuclease.Semantic proximity Read ↗

Isolation and physical characterization of random insertions in Staphylococcal nuclease.Semantic proximity Read ↗

Accommodation of insertion mutations on the surface and in the interior of staphylococcal nuclease.Semantic proximity Read ↗

Mobile unnatural amino acid side chains in the core of staphylococcal nuclease.Semantic proximity Read ↗

Mutations can cause large changes in the conformation of a denatured protein.Semantic proximity Read ↗

Proteins with simplified hydrophobic cores compared to other packing mutants.Semantic proximity Read ↗

Local stability identification and the role of key acidic amino acid residues in staphylococcal nuclease unfolding.Semantic proximity Read ↗

Deletion of the omega-loop in the active site of staphylococcal nuclease. 2. Effects on protein structure and dynamics.Semantic proximity Read ↗

Increasing the thermostability of staphylococcal nuclease: implications for the origin of protein thermostability.Semantic proximity Read ↗

A dynamic bundle of four adjacent hydrophobic segments in the denatured state of staphylococcal nuclease.Semantic proximity Read ↗

In a staphylococcal nuclease mutant the side-chain of a lysine replacing valine 66 is fully buried in the hydrophobic core.Semantic proximity Read ↗

NMR structure of a stable "OB-fold" sub-domain isolated from staphylococcal nuclease.Semantic proximity Read ↗

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