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  • Calmodulin  (1)
  • molecular recognition  (1)
  • protein-protein interaction  (1)
  • 1
    ISSN: 1570-0267
    Keywords: calcium signaling ; EF-hand protein ; molecular recognition ; protein-protein interaction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The intracellular calcium sensor protein calmodulin (CaM) interacts with a large number of proteins to regulate their biological functions in response to calcium stimulus. This molecular recognition process is diverse in its mechanism, but can be grouped into several classes based on structural and sequence information. We have developed a web-based database ( for this family of proteins containing CaM binding sites or, as we propose to call it herein, CaM recruitment signaling (CRS) motifs. At present the CRS motif found in approximately 180 protein sequences in the databases can be divided into four subclasses, each subclass representing a distinct structural mode of molecular recognition involving CaM. The database can predict a putative CRS location within a given protein sequence, identify the subclass to which it may belong, and structural and biophysical parameters such as hydrophobicity, hydrophobic moment, and propensity for a -helix formation.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-1017
    Keywords: Calmodulin ; Calmodulin fragments ; FTIR spectroscopy ; Ca2+-binding effects
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract Fourier transform infrared spectra were obtained for mammalian calmodulin and two of its fragments produced by limited proteolysis with trypsin TR1C (1–77) and TR2C (78–148). Experiments were done in H2O, D2O and D2O/trifluoroethanol (TFE) mixtures. Information about secondary structure was obtained from analysis of the amide I and II bands; while characteristic absorbances for tyrosine, phenylalanine and carboxylate groups were analyzed for changes in tertiary structure. Our data indicate that the secondary and tertiary structure is preserved in the two half molecules of CaM, both in the apo- and Ca2+-saturated state. Addition of the structure-inducing solvent TFE causes marked changes only in the apo-TR1C domain. The maximum wavenumber for the amide I band of the two domains of CaM in D20 was markedly different (1642 cm−1 for TR1C versus 1646/1648 cm−1 for Ca 2+ and apo-TR2C). This renders the amide I band for the intact protein very broad in comparison to that in other proteins and is indicative of a distribution of α-helices with slightly different hydrogen bonding patterns.
    Type of Medium: Electronic Resource
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