UNSPECIFIED. (2003) Relative affinity constants by electrospray ionization and Fourier transform ion cyclotron resonance mass spectrometry: Calmodulin binding to peptide analogs of myosin light chain kinase. BIOPHYSICAL JOURNAL, 85 (1). pp. 491-500. ISSN 0006-3495

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Abstract

Synthetic RS20 peptide and a set of its point-mutated peptide analogs have been used to analyze the interactions between calmodulin (CaM) and the CaM-binding sequence of smooth-muscle myosin light chain kinase both in the presence and the absence of Ca2+. Particular peptides, which were expected to have different binding strengths, were chosen to address the effects of electrostatic and bulky mutations on the binding affinity of the RS20 sequence. Relative affinity constants for protein/ligand interactions have been determined using electrospray ionization and Fourier transform ion cyclotron resonance mass spectrometry. The results evidence the importance of electrostatic forces in interactions between CaM and targets, particularly in the presence of Ca2+, and the role of hydrophobic forces in contributing additional stability to the complexes both in the presence and the absence of Ca2+.

Item Type:	Journal Article
Subjects:	Q Science > QH Natural history > QH301 Biology
Journal or Publication Title:	BIOPHYSICAL JOURNAL
Publisher:	BIOPHYSICAL SOCIETY
ISSN:	0006-3495
Date:	July 2003
Volume:	85
Number:	1
Number of Pages:	10
Page Range:	pp. 491-500
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/9624

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