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Relative affinity constants by electrospray ionization and Fourier transform ion cyclotron resonance mass spectrometry: calmodulin binding to peptide analogs of myosin light chain kinase
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Nousiainen, Marjaana, Derrick, Peter J. , Lafitte, Daniel and Vainiotalo, Pirjo (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, Vol.85 (No.1). pp. 491-500. doi:10.1016/S0006-3495(03)74494-4 ISSN 0006-3495.
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Official URL: http://dx.doi.org/10.1016/S0006-3495(03)74494-4
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 | ||||
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Subjects: | Q Science > QD Chemistry | ||||
Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry | ||||
Library of Congress Subject Headings (LCSH): | Ion cyclotron resonance spectrometry, Electrospray ionization mass spectrometry, Fourier transform nuclear magnetic resonance spectroscopy, Peptides -- Analysis, Electrostatics | ||||
Journal or Publication Title: | Biophysical Journal | ||||
Publisher: | Biophysical Society | ||||
ISSN: | 0006-3495 | ||||
Official Date: | July 2003 | ||||
Dates: |
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Volume: | Vol.85 | ||||
Number: | No.1 | ||||
Page Range: | pp. 491-500 | ||||
DOI: | 10.1016/S0006-3495(03)74494-4 | ||||
Status: | Peer Reviewed | ||||
Access rights to Published version: | Open Access (Creative Commons) | ||||
Funder: | Engineering and Physical Sciences Research Council (EPSRC), Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), Graduate School in Chemical Engineering (Finland) (GSCE) | ||||
Grant number: | 88/9708907 (BBSRC), |
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