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

Backbone dynamics and energetics of a calmodulin domain mutant exchanging between closed and open conformations.

Journal of molecular biology - 11 Jun 1999

Evenäs J, Forsén S, Malmendal A, Akke M

Abstract excerpt

Previous studies have suggested that the Ca2+-saturated E140Q mutant of the C-terminal domain of calmodulin exhibits equilibrium exchange between "open" and "closed" conformations similar to those of the Ca2+-free and Ca2+-saturated states of wild-type calmodulin. The backbone dynamics of this mutant were studied using15N spin relaxation experiments at three different temperatures. Measurements at each...

Read the complete abstract on PubMed

Topics

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

Share to Calmodulin
Share to Magnetic Resonance Spectroscopy
Share to Models, Molecular

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

Share to Mutation

Share to Nitrogen Isotopes

Share to Protein Conformation

Share to Temperature

Source

Identifiers

PMID: 10356332
DOI: 10.1006/jmbi.1999.2770

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

Backbone dynamics and energetics of a calmodulin domain mutant exchanging between closed and open conformations.PMID 10356332Read ↗

Dynamics of the transition between open and closed conformations in a calmodulin C-terminal domain mutant.Semantic proximity Read ↗

Quantitative analysis of conformational exchange contributions to 1H-15N multiple-quantum relaxation using field-dependent measurements. Time scale and structural characterization of exchange in a calmodulin C-terminal domain mutant.Semantic proximity Read ↗

Paramecium calmodulin mutants defective in ion channel regulation can bind calcium and undergo calcium-induced conformational switching.Semantic proximity Read ↗

Ligand-linked stability of mutants of the C-domain of calmodulin.Semantic proximity Read ↗

Arrhythmogenic calmodulin variants D131E and Q135P disrupt interaction with the L-type voltage-gated Ca2+ channel (Cav1.2) and reduce Ca2+-dependent inactivation.Semantic proximity Read ↗

Changes in the dynamics of the cardiac troponin C molecule explain the effects of Ca2+-sensitizing mutations.Semantic proximity Read ↗

Sampling unfolding intermediates in calmodulin by single-molecule spectroscopy.Semantic proximity Read ↗

Characterization of the N-terminal half-saturated state of calbindin D9k: NMR studies of the N56A mutant.Semantic proximity Read ↗

Phenylalanine fluorescence studies of calcium binding to N-domain fragments of Paramecium calmodulin mutants show increased calcium affinity correlates with increased disorder.Semantic proximity Read ↗

Structural dynamics of calmodulin-ryanodine receptor interactions: electron paramagnetic resonance using stereospecific spin labels.Semantic proximity Read ↗

Ca2+ binding in proteins of the calmodulin superfamily: cooperativity, electrostatic contributions and molecular mechanisms.Semantic proximity Read ↗

Tuning the affinity for lanthanides of calcium binding proteins.Semantic proximity Read ↗

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