AbstractMolecular dynamics studies of the N-domain (amino acids 1–77; CaM1−77) of Ca2+-loaded calmodulin (CaM) show that a solvent exposed hydrophobic cleft in the crystal structure of CaM exhibits transitions from an exposed (open) to a buried (closed) state over a time scale of nanoseconds. As a consequence of burying the hydrophobic cleft, the Rg of the protein is reduced by 1.5Å. Based on this prediction, x-ray scattering experiments were conducted on this domain over a range of concentrations. Models built from the scattering data show that the Rg and general shape is consistent with the simulation studies of CaM1−77. Based on these observations we postulate a model in which the conformation of CaM fluctuates between two different stat...
AbstractBackground: Calmodulin is a ubiquitous Ca2+-activated regulator of cellular processes in euk...
Double mutation of Q41L and K75I in the N-domain of calmodulin (N-Cam) stabilizes the closed form of...
AbstractCalmodulin (CaM) is a highly flexible calcium-binding protein that mediates signal transduct...
AbstractMolecular dynamics studies of the N-domain (amino acids 1–77; CaM1−77) of Ca2+-loaded calmod...
AbstractTo characterize the dynamic behavior of calmodulin in solution, we have carried out molecula...
AbstractA 20-ns molecular dynamics simulation of Ca2+-calmodulin (CaM) in explicit solvent is descri...
AbstractRecent high-resolution crystal and solution structures have answered many long-standing ques...
ABSTRACT To characterize the dynamic behavior of calmodulin in solution, we have carried out molecul...
AbstractMolecular dynamics simulations were performed to simulate Ca2+-dependent conformational chan...
<div><p>Calmodulin (CaM) is a calcium sensing protein that regulates the function of a large number ...
Calmodulin (CaM) is an intracellular cooperative calcium-binding protein essential for activating ma...
The fold of calmodulin (CaM) consists of two globular domains connected by a helical segment (the li...
AbstractDynamic light scattering (DLS) has been used to assess the influence of eleven different syn...
Calmodulin (CaM) is a highly conserved eukaryotic Ca2+ sensor protein that is able to bind a large v...
We present the results of computational simulation studies of the structures of calmodulin (CAM) and...
AbstractBackground: Calmodulin is a ubiquitous Ca2+-activated regulator of cellular processes in euk...
Double mutation of Q41L and K75I in the N-domain of calmodulin (N-Cam) stabilizes the closed form of...
AbstractCalmodulin (CaM) is a highly flexible calcium-binding protein that mediates signal transduct...
AbstractMolecular dynamics studies of the N-domain (amino acids 1–77; CaM1−77) of Ca2+-loaded calmod...
AbstractTo characterize the dynamic behavior of calmodulin in solution, we have carried out molecula...
AbstractA 20-ns molecular dynamics simulation of Ca2+-calmodulin (CaM) in explicit solvent is descri...
AbstractRecent high-resolution crystal and solution structures have answered many long-standing ques...
ABSTRACT To characterize the dynamic behavior of calmodulin in solution, we have carried out molecul...
AbstractMolecular dynamics simulations were performed to simulate Ca2+-dependent conformational chan...
<div><p>Calmodulin (CaM) is a calcium sensing protein that regulates the function of a large number ...
Calmodulin (CaM) is an intracellular cooperative calcium-binding protein essential for activating ma...
The fold of calmodulin (CaM) consists of two globular domains connected by a helical segment (the li...
AbstractDynamic light scattering (DLS) has been used to assess the influence of eleven different syn...
Calmodulin (CaM) is a highly conserved eukaryotic Ca2+ sensor protein that is able to bind a large v...
We present the results of computational simulation studies of the structures of calmodulin (CAM) and...
AbstractBackground: Calmodulin is a ubiquitous Ca2+-activated regulator of cellular processes in euk...
Double mutation of Q41L and K75I in the N-domain of calmodulin (N-Cam) stabilizes the closed form of...
AbstractCalmodulin (CaM) is a highly flexible calcium-binding protein that mediates signal transduct...