Evaluation of heat-induced conformational changes in proteins by nanoelectrospray Fourier transform ion cyclotron resonance mass spectrometry

1998 ◽  
Vol 4 (1) ◽  
pp. 401 ◽  
Author(s):  
Thilo Fligge ◽  
Michael Przybylski ◽  
John Quinn ◽  
Alan Marshall
2007 ◽  
Vol 13 (4) ◽  
pp. 281-290 ◽  
Author(s):  
Petr Novak ◽  
Vladimir Havlicek ◽  
Peter J. Derrick ◽  
Kyle A. Beran ◽  
Sajid Bashir ◽  
...  

Calmodulin is an EF hand calcium binding protein. Its binding affinities to various protein/peptide targets often depend on the conformational changes induced by the binding of calcium. One such target is melittin, which binds tightly to calmodulin in the presence of calcium, and inhibits its function. Chemical cross-linking combined with Fourier transform ion cyclotron resonance mass spectrometry has been employed to investigate the coordination of calmodulin and melittin in the complex at different concentrations of calcium. This methodology can be used to monitor structural changes in proteins induced by ligand binding and to study the effects these changes have on non-covalent interactions between proteins. Cross-linking results indicate that the binding place of the first melittin in the calcium-free calmodulin form is the same as in the calcium-loaded calmodulin/melittin complex.


2021 ◽  
Author(s):  
Konstantin O. Nagornov ◽  
Oleg Y. Tsybin ◽  
Edith Nicol ◽  
Anton N. Kozhinov ◽  
Yury O. Tsybin

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