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

Native-like partially folded conformations and folding process revealed in the N-terminal large fragments of staphylococcal nuclease: a study by NMR spectroscopy.

Journal of molecular biology - 18 Jul 2003

Feng Yingang, Liu Dongsheng, Wang Jinfeng

Abstract excerpt

The N-terminal large fragments of staphylococcal nuclease (SNase), SNase110 (1-110 residues), SNase121 (1-121 residues), and SNase135 (1-135 residues), and the fragment mutants G88W110, G88W121, V66W110 and V66W121 were studied by heteronuclear multidimensional NMR spectroscopy. Ensembles of co-existent native-like partially folded and unfolded states were observed for fragments. The persistent native-like...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Magnetic Resonance Spectroscopy

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

Share to Micrococcal Nuclease

Share to Models, Molecular

Share to Mutation

Share to Protein Conformation

Share to Protein Folding

Share to Protein Structure, Tertiary

Source

Identifiers

PMID: 12850150
DOI: 10.1016/s0022-2836(03)00660-0

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

Native-like partially folded conformations and folding process revealed in the N-terminal large fragments of staphylococcal nuclease: a study by NMR spectroscopy.PMID 12850150Read ↗

Effect of a specific hydrogen bond (N138ND2-Q106O) on conformational integrity, stability, and activity of staphylococcal nuclease.Semantic proximity Read ↗

Sensitivity of NMR residual dipolar couplings to perturbations in folded and denatured staphylococcal nuclease.Semantic proximity Read ↗

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

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

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

Staphylococcal nuclease folding intermediate characterized by hydrogen exchange and NMR spectroscopy.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 ↗

Proline isomerism in staphylococcal nuclease characterized by NMR and site-directed mutagenesis.Semantic proximity Read ↗

Nonlocal interactions are responsible for tertiary structure formation in staphylococcal nuclease.Semantic proximity Read ↗

Subdomain-specific collapse of denatured staphylococcal nuclease revealed by single molecule fluorescence resonance energy transfer measurements.Semantic proximity Read ↗

The Structural and Dynamical Properties of the Hydration of SNase Based on a Molecular Dynamics Simulation.Semantic proximity Read ↗

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

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