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Isotope-edited Fourier transform infrared spectroscopy studies of calmodulin's interaction with its target peptides.

Abstract：

:The ubiquitous calcium-binding protein calmodulin (CaM) regulates a wide variety of cellular events by binding to and activating many distinct target enzymes. The CaM-binding domains of most of these enzymes are contained in a contiguous stretch of amino acids with a length of approximately 20 residues. In this work, we have used "isotope-edited" Fourier transform infrared spectroscopy to study the interaction of CaM with synthetic peptides resembling the CaM-binding domains of myosin light chain kinase (MLCK), constitutive nitric oxide synthase (cNOS), and caldesmon (CaD). Uniform labeling of CaM with carbon-13 causes the amide I band of the protein to shift approximately 55 cm-1 to lower frequency in D2O, leaving a clear window in the infrared spectrum for observing the amide I band of the unlabeled target peptides. Upon complex formation, the amide I bands of the CaM-binding domains of MLCK and cNOS shift 4 cm-1 toward higher frequency (to approximately 1648 cm-1), and have a narrower bandwidth compared to the peptide in aqueous solution. These spectral changes and the fact that the infrared spectra of these two peptides in their complex with CaM closely resemble those recorded in a mixture of D2O and the helix inducing solvent trifluoroethanol indicate that they bind to CaM in an alpha-helical conformation. The CaM-binding domain of CaD also showed similar, but less dramatic, spectral changes; this is in agreement with the fact that it binds to CaM with lower affinity and a shorter alpha-helix.(ABSTRACT TRUNCATED AT 250 WORDS)

journal_name

Biochemistry

journal_title

Biochemistry

authors

Zhang M,Fabian H,Mantsch HH,Vogel HJ

doi

10.1021/bi00202a006

subject

Has Abstract

pub_date

1994-09-13 00:00:00

pages

10883-8

issue

36

eissn

0006-2960

issn

1520-4995

journal_volume

33

pub_type

杂志文章

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