ArticleProceedings of the National Academy of Sciences of the United States of America2012
Calcium-dependent folding of single calmodulin molecules.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- Acbd7 is essential for preserving hair cell-mediated auditory and vestibular function.Experimental & molecular medicine · 2026Article
- Neurogranin-MYH9 interaction regulates cytoskeletal remodeling in cerebral vasculature.Fluids and barriers of the CNS · 2025Article
- Calcium transients regulate the apical emergence of basally located progenitors during Xenopus skin development.Nature communications · 2025Article
- Binding Energy and Free Energy of Calcium Ion to Calmodulin EF-Hands with the Drude Polarizable Force Field.ACS physical chemistry Au · 2022Article
- Unraveling the Mechanics of a Repeat-Protein Nanospring: From Folding of Individual Repeats to Fluctuations of the Superhelix.ACS nano · 2022Article
- Detection of weak non-covalent cation-π interactions in NGAL by single-molecule force spectroscopy.Nano research · 2022Article
- Properties of Calmodulin Binding to NaNeurochemical research · 2021Article
- Identification and Physicochemical Characterization of a New Allergen fromInternational journal of molecular sciences · 2020Article
- Mitochondrial Metabolism, Contact Sites and Cellular Calcium Signaling: Implications for Tumorigenesis.Cancers · 2020Review
- Uncovering the Early Stages of Domain Melting in Calmodulin with Ultrafast Temperature-Jump Infrared Spectroscopy.The journal of physical chemistry. B · 2019Article
- Consequences of Hydrophobic Nanotube Binding on the Functional Dynamics of Signaling Protein Calmodulin.ACS omega · 2019Article
- Non-equilibrium dynamics of a nascent polypeptide during translation suppress its misfolding.Nature communications · 2019Article
- The Effect of CaInternational journal of molecular sciences · 2018Article
- Cotranslocational processing of the protein substrate calmodulin by an AAA+ unfoldase occurs via unfolding and refolding intermediates.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Gold nanocrystal labels provide a sequence-to-3D structure map in SAXS reconstructions.Science advances · 2018Article
- The Complex Conformational Dynamics of Neuronal Calcium Sensor-1: A Single Molecule Perspective.Frontiers in molecular neuroscience · 2018Review
- Calmodulinopathy: Functional Effects of CALM Mutations and Their Relationship With Clinical Phenotypes.Frontiers in cardiovascular medicine · 2018Review
- Calmodulinopathy: A Novel, Life-Threatening Clinical Entity Affecting the Young.Frontiers in cardiovascular medicine · 2018Review
- Single-Molecule Protein Folding Experiments Using High-Precision Optical Tweezers.Methods in molecular biology (Clifton, N.J.) · 2017Article
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2 authors.
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Abstract
Calmodulin is the primary calcium binding protein in living cells. Its function and structure depend strongly on calcium concentration. We used single molecule force spectroscopy by optical tweezers to study the folding of calmodulin in the physiologically relevant range. We find that full-length calmodulin switches from a rich and complex folding behavior at high calcium to a simple folding pathway at apo conditions. Using truncation mutants, we studied the individual domains separately. Folding and stability of the individual domains differ significantly at low calcium concentrations. With increasing calcium, the folding rate constants increase while unfolding rate constants decrease. The complete kinetic as well as energetic behavior of both domains could be modeled using a calcium-dependent three-pathway model. We find that the dominant folding pathway at high calcium concentrations proceeds via a transition state capable of binding one calcium ion. The folding of calmodulin seems to be designed to occur fast robustly over a large range of calcium concentrations and hence energetic stabilities.
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