Steered molecular dynamics and mechanical functions of proteins.
Atomic force microscopy of single molecules, steered molecular dynamics and the theory of stochastic processes have established a new field that investigates mechanical functions of proteins, such as ligand-receptor binding/unbinding and elasticity of muscle proteins during stretching. The combination of these methods yields information on the energy landscape that controls mechanical function and on the force-bearing components of proteins, as well as on the underlying physical mechanisms.
Isralewitz
B
B
Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
Gao
M
M
Schulten
K
K
D001360:Avidin / Q000737:chemistry / Q000378:metabolism; D001710:Biotin / Q000737:chemistry / Q000378:metabolism; D003198:Computer Simulation; D064211:Connectin; D005353:Fibronectins / Q000737:chemistry / Q000378:metabolism; D007136:Immunoglobulins / Q000737:chemistry / Q000378:metabolism; D018625:Microscopy, Atomic Force / Q000379:methods*; D009124:Muscle Proteins / Q000737:chemistry / Q000378:metabolism; D011494:Protein Kinases / Q000737:chemistry / Q000378:metabolism; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*
D064211:Connectin; D005353:Fibronectins; D007136:Immunoglobulins; D009124:Muscle Proteins; D011506:Proteins; D001360:Avidin; D001710:Biotin; D011494:Protein Kinases