ArticleProtein science : a publication of the Protein Society2001
Solvation energetics and conformational change in EF-hand proteins.
Article in Protein science : a publication of the Protein Society, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 48 citations in OpenAlex.
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- Development and Applications of a Calmodulin-Based Fusion Protein System for the Expression and Purification of WW and Zinc Finger Modules.Advances in biological chemistry · 2017Article
- Pathogenesis associated with a restrictive cardiomyopathy mutant in cardiac troponin T is due to reduced protein stability and greatly increased myofilament Ca2+ sensitivity.Biochimica et biophysica acta · 2015Article
- Modulation of calmodulin lobes by different targets: an allosteric model with hemiconcerted conformational transitions.PLoS computational biology · 2015Article
- A high-resolution structure of the EF-hand domain of human polycystin-2.Protein science : a publication of the Protein Society · 2014Article
- Functional and structural analysis of the conserved EFhd2 protein.Protein and peptide letters · 2013Article
- Relating form and function of EF-hand calcium binding proteins.Accounts of chemical research · 2011Article
- Thermodynamic basis for the optimization of binding-induced biomolecular switches and structure-switching biosensors.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Rational design of a conformation-switchable Ca2+- and Tb3+-binding protein without the use of multiple coupled metal-binding sites.The FEBS journal · 2008Article
- Article
- The change of protein intradomain mobility on ligand binding: is it a commonly observed phenomenon?Biophysical journal · 2006Article
- Use of sequence duplication to engineer a ligand-triggered, long-distance molecular switch in T4 lysozyme.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- A molecular dynamics study of Ca(2+)-calmodulin: evidence of interdomain coupling and structural collapse on the nanosecond timescale.Biophysical journal · 2004Article
- Energy functions for protein design I: efficient and accurate continuum electrostatics and solvation.Protein science : a publication of the Protein Society · 2004Article
- Calcium binding to calmodulin mutants monitored by domain-specific intrinsic phenylalanine and tyrosine fluorescence.Biophysical journal · 2002Article
- Origins of the difference in Ca2+ requirement for activation of mu- and m-calpain.The Biochemical journal · 2002Article
- Conformational and thermodynamic properties of peptide binding to the human S100P protein.Protein science : a publication of the Protein Society · 2002Article
- The EF-hand domain: a globally cooperative structural unit.Protein science : a publication of the Protein Society · 2002Article
- Phenylalanine fluorescence studies of calcium binding to N-domain fragments of Paramecium calmodulin mutants show increased calcium affinity correlates with increased disorder.Protein science : a publication of the Protein Society · 2001Article
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2 authors at 1 institution in 1 country.
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Abstract
Calmodulin and other members of the EF-hand protein family are known to undergo major changes in conformation upon binding Ca(2+). However, some EF-hand proteins, such as calbindin D9k, bind Ca(2+) without a significant change in conformation. Here, we show the importance of a precise balance of solvation energetics to conformational change, using mutational analysis of partially buried polar groups in the N-terminal domain of calmodulin (N-cam). Several variants were characterized using fluorescence, circular dichroism, and NMR spectroscopy. Strikingly, the replacement of polar side chains glutamine and lysine at positions 41 and 75 with nonpolar side chains leads to dramatic enhancement of the stability of the Ca(2+)-free state, a corresponding decrease in Ca(2+)-binding affinity, and an apparent loss of ability to change conformation to the open form. The results suggest a paradigm for conformational change in which energetic strain is accumulated in one state in order to modulate the energetics of change to the alternative state.
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