Conformational switching in muscle.
Muscles can be studied as complex systems of many interacting proteins and investigated at many different levels of organization. This talk will describe how we modeled the mechanism of Ca activation, the structure of the muscle proteins, and protein complexes (including actin monomers, tropomyosin and troponin complexes, and myosin) to examine two different scientific problems: the mechano-chemical energy transduction mechanism, and the control system of that mechanism. The methods we used--saturation transfer electron paramagnetic resonance, phosphorescence anisotropy, and fluorescence resonance energy transfer--reveal two specific structures: a hinge between the motor and regulatory domains, and a stiff regulatory domain. This indicates that the structure of the myosin head is capable of generating translating conformational changes within the motor domain to the swing of the regulatory domain, and that the regulatory domain is rigid enough to act as a lever arm.
Fajer
Piotr
P
Florida State University, Tallahassee, FL 32310, USA.
D001665:Binding Sites; D040542:Mechanotransduction, Cellular / Q000502:physiology; D008954:Models, Biological; D008956:Models, Chemical; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000502:physiology*; D009068:Movement / Q000502:physiology; D009119:Muscle Contraction / Q000502:physiology*; D009124:Muscle Proteins / Q000737:chemistry* / Q000502:physiology*; D018482:Muscle, Skeletal / Q000737:chemistry* / Q000502:physiology*; D009218:Myosins / Q000737:chemistry / Q000502:physiology; D011485:Protein Binding; D011487:Protein Conformation; D013057:Spectrum Analysis / Q000379:methods; D013329:Structure-Activity Relationship; D014336:Troponin / Q000737:chemistry / Q000502:physiology
D020409:Molecular Motor Proteins; D009124:Muscle Proteins; D014336:Troponin; D009218:Myosins