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Calcium-Dependent Interactions of Calmodulin with Select Peptides: A Comprehensive Study

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This study investigates the dependence of calmodulin (CaM) on calcium ions (Ca2+) and its interactions with specific peptides (Pep.G, Pep.H, Pep.I, Pep.J). The experiments utilize varying concentrations of free Ca2+ (200 μM) and complexing agents like EGTA. Response patterns and binding affinities are analyzed for CaM and peptide complexes, examining the roles of peptide sequences P62, P63, P64, and P65. Results elucidate the influence of calcium on peptide binding and suggest potential implications for calcium signaling pathways in cellular processes.

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Calcium-Dependent Interactions of Calmodulin with Select Peptides: A Comprehensive Study

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  1. ATP dependence Ca2+ dependence CaM1234

  2. CaM Pep G Pep H Pep I Pep J CaM Pep G Pep H Pep I Pep J CaM Pep G Pep H Pep I Pep J CaM Pep G Pep H Pep I Pep J P62 P63 P64 P65 CaM P62 P63 P64 P65 CaM 200 M free Ca2+ CaM:peptide 1:8 1 mM EGTA CaM:peptide 1:8 1 mM EGTA CaM:peptide 1:8 1 mM EGTA CaM:peptide 1:8 P62 P63 P64 P65 CaM1234 P62 P63 P64 P65 CaM1234 200 M free Ca2+ CaM1234:peptide 1:8 1 mM EGTA CaM1234:peptide 1:8

  3. EGTA Ca2+ Suramin Suramin CaM CaM CaM CaM 50 µM 50 µM 0 µM 25 µM 100 µM 0 µM 25 µM 100 µM 50 µM 50 µM 0 µM 25 µM 100 µM 0 µM 25 µM 100 µM P13 P14 P14 P13

  4. IP3R3 1-225

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