ArticleBiophysical journal2005
Electrostatic contributions to the kinetics and thermodynamics of protein assembly.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 44 citations in OpenAlex.
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- Autosomal Dominant Gyrate Atrophy-Like Choroidal Dystrophy Revisited: 45 Years Follow-Up and Association with a NovelInternational journal of molecular sciences · 2021Article
- Benefits and constrains of covalency: the role of loop length in protein stability and ligand binding.Scientific reports · 2020Article
- Trodusquemine enhances AβNature communications · 2019Article
- Engineering Human Epidermal Growth Receptor 2-Targeting Hepatitis B Virus Core Nanoparticles for siRNA DeliveryACS applied nano materials · 2018Article
- Modulation of electrostatic interactions to reveal a reaction network unifying the aggregation behaviour of the Aβ42 peptide and its variants.Chemical science · 2017Article
- Charge density distributions derived from smoothed electrostatic potential functions: design of protein reduced point charge models.Journal of computer-aided molecular design · 2011Article
- Calcium binding, structural stability and guanylate cyclase activation in GCAP1 variants associated with human cone dystrophy.Cellular and molecular life sciences : CMLS · 2010Article
- Green fluorescence induced by EF-hand assembly in a split GFP system.Protein science : a publication of the Protein Society · 2009Article
- Protein GB1 folding and assembly from structural elements.International journal of molecular sciences · 2009Article
- In silico screening of mutational effects on enzyme-proteic inhibitor affinity: a docking-based approach.BMC structural biology · 2007Article
- Classical nucleation theory of virus capsids.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
The role of electrostatic interactions in the assembly of a native protein structure was studied using fragment complementation. Contributions of salt, pH, or surface charges to the kinetics and equilibrium of calbindin D(9k) reconstitution was measured in the presence of Ca(2+) using surface plasmon resonance and isothermal titration calorimetry. Whereas surface charge substitutions primarily affect the dissociation rate constant, the association rates are correlated with subdomain net charge in a way expected for Coulomb interactions. The affinity is reduced in all mutants, with the largest effect (260-fold) observed for the double mutant K25E+K29E. At low net charge, detailed charge distribution is important, and charges remote from the partner EF-hand have less influence than close ones. The effects of salt and pH on the reconstitution are smaller than mutational effects. The interaction between the wild-type EF-hands occurs with high affinity (K(A) = 1.3 x 10(10) M(-1); K(D) = 80 pM). The enthalpy of association is overall favorable and there appears to be a very large favorable entropic contribution from the desolvation of hydrophobic surfaces that become buried in the complex. Electrostatic interactions contribute significantly to the affinity between the subdomains, but other factors, such as hydrophobic interactions, dominate.
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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.