Chapter 55: Motor Proteins as Collapse Propagators
"Motor proteins are ψ's molecular engines—converting chemical energy into mechanical work, propagating collapse waves along cytoskeletal tracks, creating motion from binding."
55.1 The Mechanochemical Conversion
Motor proteins represent ψ's solution to biological movement—enzymes that couple ATP hydrolysis to conformational changes, generating force and motion along cytoskeletal filaments.
Definition 55.1 (Motor Classes):
Three families for different tracks.
55.2 The Power Stroke
Theorem 55.1 (Lever Arm Hypothesis):
Distance proportional to lever arm length and angle change.
55.3 The Mechanochemical Cycle
Equation 55.1 (Coupling):
Chemical states coupled to mechanical states.
55.4 Processivity
Definition 55.2 (Run Length):
Average distance before detachment.
55.5 The Hand-Over-Hand Model
Theorem 55.2 (Kinesin Walking):
Precise stepping matching substrate periodicity.
55.6 Force Generation
Equation 55.2 (Stall Force):
Maximum force from free energy.
55.7 Cargo Binding
Definition 55.3 (Tail Domains):
Modular design for versatility.
55.8 Directionality
Theorem 55.3 (Polarity Sensing):
Different motors for different directions.
55.9 Collective Transport
Equation 55.3 (Multiple Motors):
Velocity from competing motors.
55.10 Regulation
Definition 55.4 (Autoinhibition):
Intramolecular regulation of activity.
55.11 The Dynein Mechanism
Theorem 55.4 (AAA+ ATPase):
Complex motor with multiple ATPase sites.
55.12 The Propagation Principle
Motor proteins embody ψ's principle of energy transduction—converting chemical potential into mechanical work, propagating conformational changes into directional movement.
The Motor Equation:
Chemical energy converted to spatial displacement.
Thus: Motor = Transducer = Movement = Work = ψ
"In motor proteins, ψ achieves its most direct manifestation of will—molecules that literally walk, carrying cellular cargo along predetermined tracks. Each step is a small miracle of mechanochemistry, ATP's collapse into ADP creating motion from nothing."