Biology – Quantitative Biology – Biomolecules
Scientific paper
2011-05-26
Biology
Quantitative Biology
Biomolecules
Accepted to PLoS Comp Biol, 2011
Scientific paper
The flexibility in the structure of calmodulin (CaM) allows its binding to over 300 target proteins in the cell. To investigate the structure-function relationship of CaM, we combined methods of computer simulation and experiments based on circular dichroism (CD) to investigate the structural characteristics of CaM that influence its target recognition in crowded cell-like conditions. We developed a unique multiscale solution of charges computed from quantum chemistry, together with protein reconstruction, coarse-grained molecular simulations, and statistical physics, to represent the charge distribution in the transition from apoCaM to holoCaM upon calcium binding. Computationally, we found that increased levels of macromolecular crowding, in addition to calcium binding and ionic strength typical of that found inside cells, can impact the conformation, helicity and the EF hand orientation of CaM. Because EF hand orientation impacts the affinity of calcium binding and the specificity of CaM's target selection, our results may provide unique insight into understanding the promiscuous behavior of calmodulin in target selection inside cells.
Cheung Margaret S.
Czader Arkadiusz
Liang Kao-Chen
Wang Qiangguo
Waxham Neal M.
No associations
LandOfFree
The Effect of Macromolecular Crowding, Ionic Strength and Calcium Binding on Calmodulin Dynamics does not yet have a rating. At this time, there are no reviews or comments for this scientific paper.
If you have personal experience with The Effect of Macromolecular Crowding, Ionic Strength and Calcium Binding on Calmodulin Dynamics, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and The Effect of Macromolecular Crowding, Ionic Strength and Calcium Binding on Calmodulin Dynamics will most certainly appreciate the feedback.
Profile ID: LFWR-SCP-O-217147