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Calcium-dependent conformational transition of calmodulin determined by Fourier transform infrared spectroscopy.

Abstract：

:The Ca(2+)-induced conformational changes in calmodulin (CaM) were monitored by Fourier transform infrared spectroscopy (FT-IR) at different molar ratios of Ca(2+) to CaM. The results show that these changes occur in two distinctive transitions. The first transition involves significant changes in the overall secondary structure with a small gain in solvent accessibility, and is completed after the second Ca(2+) binds to both EF-hands of its C-terminal domain. The second transition is accompanied by CaM folding into a tighter, less hydrogen-exchangeable structure, and is completed by the addition of the fourth Ca(2+) to have four Ca(2+) per molecule. Particularly, α-helices in CaM-nCa(2+)(n=0, 1, 2) are less stable than those in CaM-nCa(2+)(n=3, 4).

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Yu T,Wu G,Yang H,Wang J,Yu S

doi

10.1016/j.ijbiomac.2013.02.004

subject

Has Abstract

pub_date

2013-05-01 00:00:00

pages

57-61

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(13)00056-1

journal_volume

56

pub_type

杂志文章

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