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

Confinement and Stabilization of Fyn SH3 Folding Intermediate Mimetics within the Cavity of the Chaperonin GroEL Demonstrated by Relaxation-Based NMR.

Biochemistry - 21 Feb 2017

Libich David S, Tugarinov Vitali, Ghirlando Rodolfo, Clore G Marius

Abstract excerpt

The interaction of two folding intermediate mimetics of the model protein substrate Fyn SH3 with the chaperonin GroEL, a supramolecular foldase/unfoldase machine, has been investigated by 15N relaxation-based nuclear magnetic resonance spectroscopy (lifetime line broadening, dark state exchange saturation transfer, and relaxation dispersion). The two mimetics comprise C-terminal truncations of wild-type and...

Read the complete abstract on PubMed

Topics

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

Share to Chaperonin 60
Share to Magnetic Resonance Spectroscopy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Nitrogen Isotopes

Share to Protein Conformation

Share to Protein Folding

Share to Protein Stability

Share to Proto-Oncogene Proteins c-fyn

Share to src Homology Domains

Source

Open in PubMed Open full text

Identifiers

PMID: 28156097
DOI: 10.1021/acs.biochem.6b01237
PMCID: PMC5404735

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Confinement and Stabilization of Fyn SH3 Folding Intermediate Mimetics within the Cavity of the Chaperonin GroEL Demonstrated by Relaxation-Based NMR.PMID 28156097Read ↗

Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR.Semantic proximity Read ↗

Side-chain interactions in the folding pathway of a Fyn SH3 domain mutant studied by relaxation dispersion NMR spectroscopy.Semantic proximity Read ↗

Identification of a collapsed intermediate with non-native long-range interactions on the folding pathway of a pair of Fyn SH3 domain mutants by NMR relaxation dispersion spectroscopy.Semantic proximity Read ↗

Hydration and packing along the folding pathway of SH3 domains by pressure-dependent NMR.Semantic proximity Read ↗

Non-sequence-specific interactions can account for the compaction of proteins unfolded under "native" conditions.Semantic proximity Read ↗

Phi-value analysis of a three-state protein folding pathway by NMR relaxation dispersion spectroscopy.Semantic proximity Read ↗

Unfolded proteins and protein folding studied by NMR.Semantic proximity Read ↗

Multiple-site exchange in proteins studied with a suite of six NMR relaxation dispersion experiments: an application to the folding of a Fyn SH3 domain mutant.Semantic proximity Read ↗

Measurement of methyl group motional parameters of invisible, excited protein states by NMR spectroscopy.Semantic proximity Read ↗

Assessment of the effects of increased relaxation dispersion data on the extraction of 3-site exchange parameters characterizing the unfolding of an SH3 domain.Semantic proximity Read ↗

Gradual disordering of the native state on a slow two-state folding protein monitored by single-molecule fluorescence spectroscopy and NMR.Semantic proximity Read ↗

Separating degenerate (1)H transitions in methyl group probes for single-quantum (1)H-CPMG relaxation dispersion NMR spectroscopy.Semantic proximity Read ↗

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