The crystal structure of calcium-calmodulin (CaM) reveals a protein with a typical dumbbell structure. Various spectroscopic studies have suggested that the central linker region of CaM, which is alpha-helical in the crystal structure, is flexible in solution. In particular, NMR studies have indicated the presence of a flexible backbone between residues Lys 77 and Asp 80. This flexibility is related directly to the function of the protein because it enables the N- and C-terminal domains of the protein to move toward each other and bind to the CaM-binding domain of a target protein. We have investigated the flexibility of the CaM central helix by a variety of computational techniques: molecular dynamics (MD) simulations, normal mode analysis...
ABSTRACT To characterize the dynamic behavior of calmodulin in solution, we have carried out molecul...
This study reveals the essence of ligand recognition mechanisms by which calmodulin (CaM) con-trols ...
The distinct character of the two calmodulin (CaM) domains is reflected in different calcium and tar...
The crystal structure of calcium-calmodulin (CaM) reveals a protein with a typical dumbbell structur...
The crystal structure of calcium-calmodulin (CaM) reveals a protein with a typical dumbbell structur...
The crystal structure of calcium-calmodulin (CaM) reveals a protein with a typical dumbbell structur...
The crystal structure of calcium-calmodulin (CaM) reveals a protein with a typical dumbbell structur...
The crystal structure of calcium-calmodulin (CaM) reveals a protein with a typical dumbbell structur...
The fold of calmodulin (CaM) consists of two globular domains connected by a helical segment (the li...
The fold of calmodulin (CaM) consists of two globular domains connected by a helical segment (the li...
The fold of calmodulin (CaM) consists of two globular domains connected by a helical segment (the li...
The fold of calmodulin (CaM) consists of two globular domains connected by a helical segment (the li...
Many protein molecules are formed by two or more domains whose structures and dynamics are closely r...
ABSTRACT To characterize the dynamic behavior of calmodulin in solution, we have carried out molecul...
AbstractA 20-ns molecular dynamics simulation of Ca2+-calmodulin (CaM) in explicit solvent is descri...
ABSTRACT To characterize the dynamic behavior of calmodulin in solution, we have carried out molecul...
This study reveals the essence of ligand recognition mechanisms by which calmodulin (CaM) con-trols ...
The distinct character of the two calmodulin (CaM) domains is reflected in different calcium and tar...
The crystal structure of calcium-calmodulin (CaM) reveals a protein with a typical dumbbell structur...
The crystal structure of calcium-calmodulin (CaM) reveals a protein with a typical dumbbell structur...
The crystal structure of calcium-calmodulin (CaM) reveals a protein with a typical dumbbell structur...
The crystal structure of calcium-calmodulin (CaM) reveals a protein with a typical dumbbell structur...
The crystal structure of calcium-calmodulin (CaM) reveals a protein with a typical dumbbell structur...
The fold of calmodulin (CaM) consists of two globular domains connected by a helical segment (the li...
The fold of calmodulin (CaM) consists of two globular domains connected by a helical segment (the li...
The fold of calmodulin (CaM) consists of two globular domains connected by a helical segment (the li...
The fold of calmodulin (CaM) consists of two globular domains connected by a helical segment (the li...
Many protein molecules are formed by two or more domains whose structures and dynamics are closely r...
ABSTRACT To characterize the dynamic behavior of calmodulin in solution, we have carried out molecul...
AbstractA 20-ns molecular dynamics simulation of Ca2+-calmodulin (CaM) in explicit solvent is descri...
ABSTRACT To characterize the dynamic behavior of calmodulin in solution, we have carried out molecul...
This study reveals the essence of ligand recognition mechanisms by which calmodulin (CaM) con-trols ...
The distinct character of the two calmodulin (CaM) domains is reflected in different calcium and tar...