ArticleBiophysical journal2004
The role of electrostatic interactions in calmodulin-peptide complex formation.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 69 citations in OpenAlex.
- The calmodulin-like proteins, CML13 and CML14 function as myosin light chains for the class XI myosins in Arabidopsis.Plant & cell physiology · 2026Article
- An integrative approach to protein sequence design through multiobjective optimization.PLoS computational biology · 2024Article
- Two MP2CL5 Antigen Vaccines from Naegleria fowleri Stimulate the Immune Response against Meningitis in the BALB/c Model.Infection and immunity · 2023Article
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- Mixed-solvent molecular dynamics simulation-based discovery of a putative allosteric site on regulator of G protein signaling 4.Journal of computational chemistry · 2021Article
- Bayesian inference of protein conformational ensembles from limited structural data.PLoS computational biology · 2018Article
- Cyanylated Cysteine Reports Site-Specific Changes at Protein-Protein-Binding Interfaces Without Perturbation.Biochemistry · 2018Article
- Local and global anatomy of antibody-protein antigen recognition.Journal of molecular recognition : JMR · 2018Article
- Development of constant-pH simulation methods in implicit solvent and applications in biomolecular systems.Biophysical reviews · 2017Review
- The Role of Solvent-Accessible Leu-208 of Cold-Active Pseudomonas fluorescens Strain AMS8 Lipase in Interfacial Activation, Substrate Accessibility and Low-Molecular Weight Esterification in the Presence of Toluene.Molecules (Basel, Switzerland) · 2017Article
- Kinetic regulation of multi-ligand binding proteins.BMC systems biology · 2016Article
- Calmodulin transduces Ca2+ oscillations into differential regulation of its target proteins.ACS chemical neuroscience · 2013Article
- Retention of conformational entropy upon calmodulin binding to target peptides is driven by transient salt bridges.Biophysical journal · 2012Article
- The motif of human cardiac myosin-binding protein C is required for its Ca2+-dependent interaction with calmodulin.The Journal of biological chemistry · 2012Article
- Structural and dynamic determinants of protein-peptide recognition.Structure (London, England : 1993) · 2011Article
- Molecular interaction and functional regulation of connexin50 gap junctions by calmodulin.The Biochemical journal · 2011Article
- Integrated protein array screening and high throughput validation of 70 novel neural calmodulin-binding proteins.Molecular & cellular proteomics : MCP · 2010Article
- Calmodulin mediates the Ca2+-dependent regulation of Cx44 gap junctions.Biophysical journal · 2009Article
- How calmodulin interacts with the adenosine A(2A) and the dopamine D(2) receptors.Journal of proteome research · 2008Article
- Elucidating the mechanisms of cooperative calcium-calmodulin interactions: a structural systems biology approach.BMC systems biology · 2008Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The complex between calmodulin and the calmodulin-binding portion of smMLCKp has been studied. Electrostatic interactions have been anticipated to be important in this system where a strongly negative protein binds a peptide with high positive charge. Electrostatic interactions were probed by varying the pH in the range from 4 to 11 and by charge deletions in CaM and smMLCKp. The change in net charge of CaM from approximately -5 at pH 4.5 to -15 at pH 7.5 leaves the binding constant virtually unchanged. The affinity was also unaffected by mutations in CaM and charge substitutions in the peptide. The insensitivity of the binding constant to pH may seem surprising, but it is a consequence of the high charge on both protein and peptide. At low pH it is further attenuated by a charge regulation mechanism. That is, the protein releases a number of protons when binding the positively charged peptide. We speculate that the role of electrostatic interactions is to discriminate against unbound proteins rather than to increase the affinity for any particular target protein.
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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.