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Increase in the molecular weight and radius of gyration of apocalmodulin induced by binding of target peptide: evidence for complex formation
Author(s) -
Izumi Yoshinobu,
Kuwamoto Shigeo,
Jinbo Yuji,
Yoshino Hidenori
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02375-4
Subject(s) - calmodulin , radius of gyration , chemistry , peptide , van der waals force , linker , residue (chemistry) , stokes radius , stereochemistry , crystallography , biophysics , molecule , biochemistry , polymer , biology , enzyme , organic chemistry , size exclusion chromatography , operating system , computer science
Small‐angle X‐ray scattering was used to investigate a complex state of apocalmodulin induced by the binding of a Ca 2+ /calmodulin‐dependent protein kinase IV calmodulin target site. Upon binding of the peptide, the molecular weight for apocalmodulin increased by 8.4%, which provides direct evidence for the formation of a calmodulin/target peptide complex. Comparison of the radius of gyration and Kratky plots of the apocalmodulin/peptide complex with those of apocalmodulin indicates that the overall conformation remains unchanged but the flexibility of the central linker decreases. An analysis of residue pairs between calmodulin and the target peptides suggests that the complex formation is induced by electrostatic interactions and subsequent van der Waals interactions.