On the molecular basis for chemomechanical energy transduction in muscle.

AUTOR(ES)

Morales, M F

RESUMO

Herein it is developed that energy transduction in muscle is an activity of myosin S-1 and its ligands, actin (A) and nucleotide (N). S-1 shares with other molecular particles (e.g., hemoglobin) the property that binding events at one of its sites, the N-site, influences binding events at a remote site, the A site (specifically, influences both the actin affinity and actin attachment angle at the A site). However, there is a crucial difference between S-1 and the better-known systems. Because the N site is enzymatic, it has a temporal sequence of occupants; this imposes a temporal sequence of actin attitudes--i.e., a sequence of mechanical events.

Documentos Relacionados

• Chemo-mechanical energy transduction in relation to myosin isoform composition in skeletal muscle fibres of the rat.
• Molecular basis of AMP deaminase deficiency in skeletal muscle.
• Effect of muscle length on energy balance in frog skeletal muscle.
• Molecular mechanism for oscillation in flagella and muscle.
• Molecular basis for decreased muscle chloride conductance in the myotonic goat.