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• W1977761296 abstract "We explore how inherent flexibility of a protein molecule influences the mechanism controlling allosteric transitions by using a variational model inspired from work in protein folding. The striking differences in the predicted transition mechanism for the opening of the two domains of calmodulin (CaM) emphasize that inherent flexibility is key to understanding the complex conformational changes that occur in proteins. In particular, the C-terminal domain of CaM (cCaM), which is inherently less flexible than its N-terminal domain (nCaM), reveals cracking or local partial unfolding during the open/closed transition. This result is in harmony with the picture that cracking relieves local stresses caused by conformational deformations of a sufficiently rigid protein. We also compare the conformational transition in a recently studied even-odd paired fragment of CaM. Our results rationalize the different relative binding affinities of the EF-hands in the engineered fragment compared with the intact odd-even paired EF-hands (nCaM and cCaM) in terms of changes in flexibility along the transition route. Aside from elucidating general theoretical ideas about the cracking mechanism, these studies also emphasize how the remarkable intrinsic plasticity of CaM underlies conformational dynamics essential for its diverse functions." @default.
• W1977761296 created "2016-06-24" @default.
• W1977761296 creator A5046973392 @default.
• W1977761296 creator A5058113729 @default.
• W1977761296 date "2009-02-17" @default.
• W1977761296 modified "2023-10-01" @default.
• W1977761296 title "Inherent flexibility determines the transition mechanisms of the EF-hands of calmodulin" @default.
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• W1977761296 doi "https://doi.org/10.1073/pnas.0806872106" @default.
• W1977761296 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2650115" @default.
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