ArticleBiophysical journal2006
A molecular dynamics study of the effect of Ca2+ removal on calmodulin structure.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 43 citations in OpenAlex.
- Metamorphic Proteins to Achieve Conformationally Selective Material Surface Binding.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Energetic and structural insights behind calcium induced conformational transition in calmodulin.Proteins · 2024Article
- The mechanism of complex formation between calmodulin and voltage gated calcium channels revealed by molecular dynamics.PloS one · 2021Article
- Coarse-Grained Modeling and Molecular Dynamics Simulations of CaFrontiers in molecular biosciences · 2021Article
- Effect of Ca2+ on the promiscuous target-protein binding of calmodulin.PLoS computational biology · 2018Article
- Origin and prediction of free-solution interaction studies performed label-free.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Internal coordinate molecular dynamics: a foundation for multiscale dynamics.The journal of physical chemistry. B · 2015Article
- Effect of Calcium Ion Removal, Ionic Strength, and Temperature on the Conformation Change in Calmodulin Protein at Physiological pH.Journal of biophysics (Hindawi Publishing Corporation : Online) · 2014Article
- Mapping conformational dynamics of proteins using torsional dynamics simulations.Biophysical journal · 2013Article
- Computational investigation of the key factors affecting the second stage activation mechanisms of domain II m-calpain.Journal of molecular modeling · 2013Article
- Designing molecular dynamics simulations to shift populations of the conformational states of calmodulin.PLoS computational biology · 2013Article
- Calcium induced regulation of skeletal troponin--computational insights from molecular dynamics simulations.PloS one · 2013Article
- Elucidating the ensemble of functionally-relevant transitions in protein systems with a robotics-inspired method.BMC structural biology · 2013Article
- Retention of conformational entropy upon calmodulin binding to target peptides is driven by transient salt bridges.Biophysical journal · 2012Article
- Article
- Protein-binding assays in biological liquids using microscale thermophoresis.Nature communications · 2010Article
- Calmodulin wraps around its binding domain in the plasma membrane Ca2+ pump anchored by a novel 18-1 motif.The Journal of biological chemistry · 2010Article
- Article
- A molecular dynamics study and free energy analysis of complexes between the Mlc1p protein and two IQ motif peptides.Biophysical journal · 2006Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Calmodulin is a small (148 residues), ubiquitous, highly-conserved Ca(2+) binding protein serving as a modulator of many calcium-dependent processes. In this study, we followed, by means of molecular dynamics, the structural stability of the protein when one of its four bound Ca(2+) ions is removed, and compared it to a simulation of the fully Ca(2+) bound protein. We found that the removal of a single Ca(2+) ion from the N-lobe of the protein, which has a lower affinity for the ion, is sufficient to initiate a considerable structural rearrangement. Although the overall structure of the fully 4 Ca(2+) bound protein remained intact in the extended conformation, the Ca(2+)-removed protein changed its conformation into a compact state. The observation that the 3 Ca(2+) loaded protein assumes a compacted solution state is in accord with experimental observation that the NSCP protein, which binds only three Ca(2+) ions, is natively in a compact state. Examination of the folding dynamics reveals a cooperation between the C-lobe, N-lobe, and the interdomain helix that enable the conformation change. The forces driving this conformational change are discussed.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.