Journal of Electromyography and Kinesiology 12 (2002) 425–433

www.elsevier.com/locate/jelekin

Considerations on muscle contraction

W. Herzog ∗, R. Ait-Haddou
Faculty of Kinesiology, University of Calgary, 2500 University Dr. N.W., Calgary, AB, Canada, T2N 1N4

Abstract

The independent force generator and the power-stroke cross-bridge model have dominated the thinking on mechanisms of muscu-
lar contraction for nearly the past five decades. Here, we review the evolution of the cross-bridge theory from its origins as a two-
state model to the current thinking of a multi-state mechanical model that is tightly coupled with the hydrolysis of ATP. Finally,
we emphasize the role of skeletal muscle myosin II as a molecular motor whose actions are greatly influenced by Brownian motion.
We briefly consider the conceptual idea of myosin II working as a ratchet rather than a power stroke model, an idea that is explored
in detail in the companion paper.
 2002 Elsevier Science Ltd. All rights reserved.

Keywords: Skeletal muscle; Sliding filament theory; Cross-bridge theory; Brownian motion; Molecular motors; Mechanisms of contraction; ATP
hydrolysis; Muscle energetics; Molecular ratchet

1. Background tein folding remained the primary mechanism for muscle

The following text is largely based on a lecture we
gave at the European Congress on Sports Science, in
Cologne, July 2001. The lecture had two principal pur-
poses. The first purpose was to provide an overview of
the current thinking governing the molecular mechanism
of muscular contraction, the cross-bridge theory, while
the second purpose was to draw attention to the limi-
tations of the current mechanism, and to propose an
alternative way of how muscular contraction might
occur. This paper will follow the same format.
Before diving into the foundations of the cross-bridge
theory, we should like to point out that the proposed
mechanism of muscular contraction has changed com-
pletely over the past century. At the beginning of the
20th century, the so-called lactic acid theory was based
on the idea that contraction was caused by the lactic
acid-induced folding of long protein chains along the
muscle fibers. This theory was disproved when it was
discovered that muscle poisoned with iodacetic acid
could produce contraction and force without lactic acid
[21]. Even with the death of the lactic acid theory, pro-
∗
Corresponding author. Tel.: +1-403-220-8525; fax: +1-403-284-
3553.
E-mail address: walter@kin.ucalgary.ca (W. Herzog).
contraction until the early 1950s.
H. Huxley [17] was the first to suggest that contraction
may occur through the relative sliding of two sets of
filaments. This so-called “sliding filament theory” was
independently confirmed by H. Huxley and Hansen [19]
and A. Huxley and Niedergerke [15] using isolated
myofibrils and phase contrast microscopy and single
fibers and interference microscopy, respectively. The
question then became, what makes filaments slide?
2. The 1957 formulation of the cross-bridge theory
In 1957, A. Huxley [13] formulated a theory that pro-
posed how filaments slide past each other. The theory
was based on several properties that had been observed
in muscle experiments. First, Ramsey and Street [27]
performed experiments on single fibers of frog and
showed that isometric force reached a maximum at an
average sarcomere length of about 2 µm. When increas-
ing the length beyond 2 µm, they found a nearly linear
decrease in force, with zero force occurring at about 4.2
µm (Fig. 1). This result suggested that force production
might be directly related to the amount of myofilament
overlap. Second, Hill [11] reported that the relationship
between the speed of shortening and the total rate of
energy liberation was a rectangular hyperbola (Fig. 2).

1050-6411/02/$ - see front matter.  2002 Elsevier Science Ltd. All rights reserved.
PII: S 1 0 5 0 - 6 4 1 1 ( 0 2 ) 0 0 0 3 6 - 6
426 W. Herzog, R. Ait-Haddou / Journal of Electromyography and Kinesiology 12 (2002) 425–433
Fig. 1. Tension developed by an isolated frog muscle fiber on stimu-
lation at different lengths. Points: Ramsey and Street [27]. Line: Ford
et al. [7] (with permission).
Fig. 2. Rates of energy liberation in excess of the steady rate during
an isometric contraction, as determined by A.V. Hill [11] (with
permission).
Needham [26] pointed out that Hill’s [11] observation
could readily be explained by active sites in a muscle
that operate in a cyclic manner, similar to an enzyme
causing a chemical reaction. Third, adenosine triphosph-
ate (ATP, Fig. 3) was discovered in muscle extracts [20],
and was shown to be hydrolyzed by actomyosin [4].
These findings hinted at the central role of ATP as the
fuel for muscle contraction.
In the formulation of the cross-bridge theory, A. Hux-
ley [13] assumed that thick filaments (myosin) had side
pieces (M) that were connected via elastic springs to the
thick filament (Fig. 4). These side pieces were thought
to oscillate about their equilibrium point (O) because of
thermal agitation (Brownian motion). Side pieces were
Fig. 3. The structure of ATP.
Fig. 4. Schematic illustration of the 1957 model of the cross-bridge
theory (adapted from Huxley [13], with permission).
assumed to attach to specialized sites (A) on the thin
filament. Attachment and detachment of the side pieces
was thought to occur in a cyclic fashion, therefore great
shortening of the muscle could occur through a series of
small steps. Each time a side piece M is attached to a
corresponding A site, force is transmitted between the
two filaments because of the force in the elastic springs
of the M piece, except if M is at its equilibrium position
where strain (and force) in the springs was assumed to
be zero.
How do we now get directed force from a system as
shown in Fig. 4. If we assume that M attaches spon-
taneously to A, as Huxley did, then one would assume
that the probability for a detached cross-bridge to attach
to an actin site is equal to the probability of its location
(x, Fig. 4). It can be shown that the probability distri-
bution of M’s location undergoing Brownian motion is
a Gaussian shape about the equilibrium position. There-
fore, a cross-bridge would likely attach to the actin at a
location where strain in the springs is relatively low, thus
force would be low as well. Similarly, from the structural
symmetry of the system, it follows that M would attach
to A with equal probability for A being located on the
left and right of the cross-bridge equilibrium position.
 W. Herzog, R. Ait-Haddou / Journal of Electromyography and Kinesiology 12 (2002) 425–433
Therefore, on average, the actin filament would undergo
a zero displacement relative to the myosin filament.
Obviously, such a system cannot produce directed mus-
cle force and shortening. In order to produce a directed
movement of actin relative to myosin (such that muscle
shortening and directed force production could occur),
Huxley [13] introduced the idea that the rate of attach-
ment (f) and detachment (g) were dependent on the x-
location (Fig. 4) of the actin attachment site relative to
the cross-bridge equilibrium position. These rate con-
stants had to be chosen asymmetrically in the sense that
the attachment probability of a cross-bridge had to be
greater for positive x-values (thus, cross-bridge attach-
ment would cause muscle shortening) than for negative
x-values. Huxley’s asymmetrical choice is shown in Fig.
5. No explanation was given as to how this asymmetry
may be produced.
If we now consider, as Huxley [13] did, a great num-
ber of M–A pairs that have one and the same x-location
at each instant in time, the proportion of attached cross-
bridges, n(x), is a function of time exclusively. By defi-
nition of f(x) and g(x), the rate of change of n(x) over
time becomes:
dn
⫽ (1⫺n)f(x)⫺ng(x) (1)
dt
For a dynamic equilibrium state (i.e., dn/dt=0), we find
that the number of attached cross-bridges, neq, is given
by the probability of attachment:
f(x)
neq ⫽ (2)
f(x) ⫹ g(x)
So far, we have assumed that all cross-bridges have the
same value x at each instant in time, t. However, for a
great number of cross-bridges, x(t) would be distributed
Fig. 5. Rate functions for the formation, f, and the breaking, g, of
cross-bridge links between the thick (myosin) and the thin (actin)
myofilaments as a function of x, the distance from the active site on
the thin filament to the equilibrium position of the cross-bridge
(adapted from Huxley [13], with permission).
427
(almost) uniformly over the range [⫺0.5la, 0.5la], where
la is the distance between actin attachment sites. The pro-
portion of attached cross-bridges, n(x, t), is now a func-
tion of x and t, and the rate of change in n(x, t) is
obtained as the material derivative:
Dn ∂n ∂n
⫽ ⫹ v (3)
Dt ∂t ∂x
where v is assumed to be negative for muscle shortening.
The governing differential equation, assuming that the
two myofilaments are perfectly rigid, becomes:
冉 冊
∂n ∂n 1
⫹ v ⫽ ⫺n f(x)⫺ng(x) (4)
∂t ∂x Ia
Eq. (4) may be solved using the method of characteristic
curves [5,35].
3. The 1969 formulation of the cross-bridge model
So far, the cross-bridge head (M, Fig. 4) was thought
to be in a single configuration. However, Reedy et al.
[30] demonstrated that cross-bridges at rest were about
perpendicular to the filament axis, while cross-bridges
in rigor were tilted 45° to the perpendicular rest con-
figuration. Based on this information, H. Huxley [18]
proposed that the cross-bridge head (subfragment 1)
attaches to the thin filament, and force and filament
transport would be generated by a tendency of the head
to rotate about its attachment point (Fig. 6). Therefore,
subfragment 1 was assumed to act as a crank, pulling
the thin relative to the thick filament. Subfragment 2,
that connects subfragment 1 to the backbone of the thick
Fig. 6. Diagram of the mechanism of force generation by a cross-
bridge as proposed by Huxley [18] (with permission).
428 W. Herzog, R. Ait-Haddou / Journal of Electromyography and Kinesiology 12 (2002) 425–433

filament, acts as a connecting rod, converting the rotary

movement of the cross-bridge head into a linear dis-
placement of the filaments. The idea of the cross-bridge
power stroke was born.

4. The 1971 formulation of the cross-bridge theory

A. Huxley and Simmons [16] observed that when a

muscle fiber is shortened rapidly, force drops virtually
simultaneously with the length change, and then recovers
in two distinct phases, a quick and a slow phase (Fig. 7).
Huxley and Simmons [16] defined the force transients
associated with a quick shortening step with two charac-
teristic variables, T1 and T2. T1 was defined as the mini-
mum force achieved during the rapid shortening step. T2
was defined as the force at the end of the quick recovery
phase. T1 was found to vary almost linearly with the
magnitude of the step, reaching zero force at a step Fig. 8. Values of T1 (the extreme tension reached after a quick short-
ening step; see Fig. 7) and T2 (the tension reached during the early
amplitude of approximately 6 nm per half-sarcomere
tension recovery after the step) as functions of the size of the step
(Fig. 8). T2 remained nearly the same as the isometric (from Ford et al. [7], with permission).
force just prior to the length step, T0, for step amplitudes
of up to about 5 nm, but then started to become progress-
ively smaller with increasing step amplitude, reaching
zero force (i.e. the early, quick recovery was completely
absent) at step amplitudes of 13 nm per half-sarcomere
and beyond.
The interpretation of these results is summarized in
the model shown in Fig. 9. The key features of this
theory are that the shortening force response is associa-
ted with an elastic element and occurs in steps. The elas-
tic element was associated with the link AB1 (AB2) in
Fig. 9, and this elastic link accounts for the virtually
instantaneous change in force with shortening (Fig. 10).
The quick recovery of force following the shortening
step was associated with a rotation of the (still attached)
cross-bridge head from a position of small affinity
between M–A attachments (M1A1) to increasingly
greater affinities between M–A for stable states M2A2, Fig. 9. Diagram to illustrate the assumptions in the theory of Huxley
and Simmons [16]. The bond between M3 and A3 is stronger than that
between M1 and A1, favoring position B2 over B1. Likewise, the bond
between M4 and A4 is stronger than that between M2 and A2. The link
AB is elastic (from Huxley and Simmons [16], with permission).

M3A3, and M4A4 (Fig. 9). Rotation of the cross-bridge

Fig. 7. Record of changes in length and tension when a sudden
decrease of length (6 nm per half-sarcomere) is imposed on an isolated
frog muscle fiber during contraction at 0 °C (from Ford et al. [7],
with permission).
head through these different attachment states would
stretch the elastic link (Fig. 10), and so provide a quick
force recovery. For step amplitudes greater than about 13
nm per half-sarcomere, all attached cross-bridges were
assumed to have detached, therefore, the quick recovery
offered by cross-bridge head rotation was lost, and only
a slow force recovery was possible that was governed
by the (slow) rate of attachment of the cross-bridges to
the actin attachment sites.
 W. Herzog, R. Ait-Haddou / Journal of Electromyography and Kinesiology 12 (2002) 425–433
Fig. 10. Schematic illustration of the presumed events associated
with a rapid release and the following quick recovery of force. (a) The
cross-bridge head is in its initial position and the elastic link is
stretched. (b) A rapid release has occurred. The cross-bridge head is
in the same orientation as in (a) but the elastic link has shortened
because of the relative movement of the myofilaments. The cross-
bridge force (carried by the elastic link) is smaller in (b) than in (a).
(c) The cross-bridge head rotates to a position of lower potential
energy, thereby stretching the elastic link and increasing the cross-
bridge force without any myofilament movement.
5. Current thinking
In the 1969 and 1971 models of the molecular mech-
anisms of contraction, cross-bridge rotation plays an
important part. This rotation was thought to occur about
429
the attachment point of the cross-bridge to actin. How-
ever, in a series of structural studies [28,29], it was sug-
gested that the connection between the cross-bridge head
(subfragment S1) and actin does not allow for rotation,
but that rotation takes place through a conformational
change of the light-chain binding domain about a hinge
within the myosin head.
Specifically, the following sequence of events was
proposed for muscular contraction (Fig. 11). Starting
Fig. 11. Proposed molecular mechanism of contraction. (A) Rigor
conformation. The narrow cleft that splits the 50 kD segments of the
myosin heavy-chain sequence into two domains is closed (horizontal
gap, perpendicular to the actin filament axis). (B) Addition of ATP,
and initial binding of ATP to the active site, causes an opening of the
narrow cleft and disrupts the strong binding between actin and myosin,
but still allows for weak binding. The actin and myosin dissociate. (C)
The final binding of ATP to myosin causes a closure of the nucleotide
binding pocket and a corresponding configurational change of the myo-
sin molecule. ATP is now hydrolyzed. (D) Myosin can now reattach
to actin, presumably in multiple steps. The narrow cleft closes to pro-
duce strong binding. Phosphate, P, is released, and the power stroke
starts. (E) During the power stroke, the myosin molecule reverses its
conformation change induced by ATP binding, the active site pocket
is reopened, ADP is released and the rigor conformation is established.
The cross-bridge cycle can now start over again. (From Rayment et
al. [29], with permission.)
430 W. Herzog, R. Ait-Haddou / Journal of Electromyography and Kinesiology 12 (2002) 425–433

from the rigor conformation, Rayment et al. [29] sug-
gested that the narrow cleft that splits the 50 kD seg-
ments of the myosin heavy chain sequence into two
domains is closed (Fig. 11A, horizontal gap, perpendicu-
lar to the actin filament axis). Addition of ATP, and
initial binding of ATP to myosin at the active site causes
an opening of the narrow cleft between the upper and
lower domains of the 50 kD segments. This event, in
turn, disrupts the “strong” binding between actin and
myosin, but still allows for a “weak” attachment (Fig.
11B). The final ATP binding to myosin causes a closure
of the nucleotide binding pocket and a corresponding
change of the myosin molecule. Myosin now detaches
from actin and ATP is hydrolyzed (Fig. 11C). Rebinding
of myosin to actin can now occur, presumably in mul-
tiple steps. The gap between the upper and lower domain
closes in this process to produce strong binding, and
phosphate, P, is released. This event starts the power
stroke (Fig. 11D). During the power stroke, the myosin
S1 reverses its conformational change induced by ATP
binding, the active site pocket is reopened, ADP is
released, and the rigor conformation is established (Fig.
11E). The cross-bridge cycle can now be restarted by
ATP binding to myosin.
The detailed reactions of myosin S1 with actin and
ATP are not known because not all of the rate constants
have been determined. However, combining the struc-
tural evidence [28,29], the biochemical data measured
in solution [2,8–10,22–24,31], and the mechanical data
[6,16], it is possible to infer the likely actin–myosin
hydrolysis cycle (Table 1). Superimposing the biochemi-
cal cycle with a schematic structural model for the
hydrolysis cycle (Fig. 12) gives the current thinking of
how muscular contraction might occur.
Starting from the top left drawing in Fig. 12, and fol-
lowing the arrows (the likely path of the actin–myosin
hydrolysis cycle), we go through the following steps.
The binding of ATP catalyzes the dissociation of myosin
from actin [3,32]. When dissociated, ATP is hydrolyzed,
and the cross-bridge head goes through a conformational
change (the recovery stroke, Fig. 12). Myosin attaches
to actin, phosphate is released, and the power or working
stroke is initiated. ADP is released, establishing the rigor
conformation. ATP then attaches to the myosin head,
myosin can now dissociate from actin, and the cycle
may restart.
Obviously, there are variations from the above pro-
posed theory of contraction, however Figs. 11 and 12,
and Table 1 represent the most accepted thinking at
present. An interesting variation of the above ideas was
proposed by A. Huxley [14] who suggested the possi-
bility of cross-bridge rotation about its attachment point
on the actin filament. Another important aspect of the
scheme discussed above is that the rate limiting step of
the cross-bridge cycle occurs in the attachment of myo-
sin to actin (Table 1). The remaining steps in the
hydrolysis cycle are considered much faster than the
attachment rate.
6. Limitations
The detailed mechanical steps of muscle contraction,
as well as the details of the actin–myosin hydrolysis
cycle are not known. And to cite A. Huxley [14]:
the whole history of muscular contraction during the
last half century shows that even when a set of ideas
seems to be well established, there is a large chance
that it will be overthrown by some unexpected dis-
covery.
With this quote in mind, we should continuously ask
ourselves, what are the limitations of the current thinking

Table 1
Actin–myosin hydrolysis cycle (rabbit skeletal muscle). (Adapted from Howard [12], with permission)

(+8 kT) (0) (⫺12 kT) (⫺15 kT) (⫺17 kT)

ⱖ104 s⫺1 103 s⫺1 20,000 s⫺1
A·M·T A·M·D·P → A·M·D , A·M , A·M·T
100s-1 2000 s⫺1
30 s⫺1 300 s⫺1 0.2 s⫺1↓ ↓1 s⫺1 0.4 s⫺1 2000 s⫺1
100 s⫺1
M·T , M·D·P → M·D M ← M·T,
10 s⫺1 0.1 s⫺1 苲10⫺4 s⫺1
(0) (⫺2 kT) (⫺8 kT) (⫺6 kT) (⫺25 kT)

M, myosin; T, ATP; D, ADP; P, phosphate; A, actin. The most commonly followed path is shown in bold type. In parentheses are the approximate
free energies of the states assuming [ATP]=4 mM, [Pi]=2 mM, [ADP]=20 µM. The actin concentration is taken to equal 1 mM, its concentration
in skeletal muscle (this is fairly arbitrary because the effective concentration in a muscle depends on the accessibility of the actin site to the myosin
head). Overall ATPase: kcat=25 s⫺1, KM(ATP)=10 µM, KM(actin)⬵100 µM (low ionic strength) at 20 °C [2]. The rate constants are based on
experimental data taken from isolated S1 and/or myofibrils under roughly physiological ionic strength. The values vary by up to a factor of 10
between laboratories. The constants (K) are dissociation constants and k+(k⫺) is the rate constant in the clockwise (counterclockwise) direction
(from Howard [12], with permission).
 W. Herzog, R. Ait-Haddou / Journal of Electromyography and Kinesiology 12 (2002) 425–433
Fig. 12. Schematic illustration of the current thinking of the cross- bridge cycle, including a best estimate of the rate constants of the reactions
(adapted from Howard [12], with permission).
on muscle contraction, and is the set of well established
ideas still the best in view of newly emerging experi-
mental results?
One of the things that has troubled us is the asym-
metry of the rate constants in a seemingly perfectly sym-
metrical model in the 1957 theory (Figs. 4 and 5). Of
course, the asymmetry was required, otherwise there
would have been no net force and no net sliding of the
actin relative to the myosin filament. However, no reason
was provided why, from a biological point of view, the
rate constants for attachment and detachment of the
cross-bridges were asymmetrical. Although, in more
recent models, structural arguments for this asymmetry
have been proposed, none seems terribly convincing.
Other questions arise from experiments on single mol-
ecules. For example, if contraction occurs as sche-
matically proposed in Figs. 11 and 12, one would expect
that the relative sliding of actin and myosin during a
single powerstroke could be calculated from the angular
reorientation and the magnitude of the lever arm. How-
ever, it is known that the myosin subfragment 1(S1) has
a shorter neck than the double-headed HMM construct.
Assuming, as has been done, that the neck region of the
cross-bridge acts as the lever arm that determines the
step size of a single power-stroke, one would expect a
smaller step size from S1 compared to HMM. However,
such a difference was not found [25]. Similarly, Yanag-
ida [33] found that step sizes remained about the same
for myosin II molecules with normal neck lengths, and
molecules in which the neck region was reduced to 20%
of its normal length. Furthermore, Yanagida [33,34]
found that myosin II had a step reversal in about 10% of
all steps observed. These results, although preliminary,
431
cannot be readily explained by a power stroke model of
muscle contraction.
As a microscopic molecular motor, the myosin head
operates at energy levels that are just a little greater than
the random thermal energy of the surroundings. These
thermal baths are essential for the process of the chemi-
cal reactions. The myosin head is exposed to these ther-
mal forces that arise from collision with molecules in
the surrounding fluid. Because of the random occurrence
of these collisions, in terms of direction and magnitude,
the cross-bridge head will undergo a random diffusion,
or Brownian motion. In the detached state, the myosin
head moves more or less freely, and therefore, undergoes
a free Brownian motion. In the attached state, the ran-
dom diffusion is limited by the force field of the actin
filament. The transition between the two diffusive modes
is driven by the chemical reaction of ATP hydrolysis.
Therefore, the movement of the cross-bridge head has
to be stochastic in nature and must be described by a
reaction–diffusion equation. Note that thermal diffusion
was part of the cross-bridge theory from its conception
[13].
At first glance, it may appear that Brownian motion
could be quite disruptive and may greatly affect the
efficiency of events such as muscular contraction. How-
ever, contrary to this intuitive thinking, it appears that
the myosin head can extract work from the thermal bath
if the system is far from equilibrium and if there is a
structural asymmetry in the geometry of the system. A
system that extracts work under these two conditions is
known as a thermal ratchet. We will investigate these
systems in much more detail in the following paper on
ratchet-type mechanisms of molecular movement,
432 W. Herzog, R. Ait-Haddou / Journal of Electromyography and Kinesiology 12 (2002) 425–433
specifically as they apply to contraction in skeletal
muscles. Ratchet-type mechanisms can work without the
assumption of asymmetry of the rate constants, an
assumption that is essential for the power-stroke cross-
bridge model. In the following, we would like to illus-
trate the role of noise in a system that is far from equilib-
rium with a simple example. The goal of this example
is to show the difference between a system in which
force is produced by a power stroke and one in which
the system extracts work from the Brownian motion.
Imagine a microscopic “being” at a starting point A
of a road, who wants to reach a point B further along
the road. Assume that the road has two parallel lanes :
One lane has wind locally, but the average wind along
the lane is zero. In the second lane, there is no wind.
The microscopic “being” is not allowed to walk on the
lane without wind. There are two strategies to reach
point B. The first strategy consists of walking forcefully
in the windy lane. The second strategy consists of stay-
ing in the lane without wind and watching the windy
lane. Every time the wind is in the required direction,
the microscopic “being” jumps into the windy lane and
takes advantage of the direction of the wind. Every time
the wind is in a direction opposite to the one the “being”
wants to go, our macroscopic friend jumps to the quiet
lane. Loosely, the first strategy is analogous to the power
stroke theory in which the energy is used directly (“pay
as you go”); and the second strategy is analogous to the
ratchet theory in which the energy is used for the switch-
ing strategy itself.
Ratchet-type mechanisms are thought to be part of
many molecular motors [1]. In the companion paper, we
explore ideas about how a ratchet mechanism may
explain the workings of skeletal muscle myosin II and
actin, i.e. muscular contraction and force production.
Acknowledgement
NSERC of Canada.
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 W. Herzog, R. Ait-Haddou / Journal of Electromyography and Kinesiology 12 (2002) 425–433 433

[31] Siemankowski RF, Wiseman MO, White HD. ADP dissociation Rachid Ait-Haddou received his MSc in
from actomyosin subfragment 1 is sufficiently slow to limit the Applied Mathematics from the University
unloaded shortening velocity in vertebrate muscle. Proc Natl Mohamed V, Rabat, Morocco, in 1991, and his
Acad Sci U S A 1985;82:658–62. PhD in Applied Mathematics from the Univer-
sity Joseph Fourier, Grenoble, France, in 1996.
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He is currently a postdoctoral scientist wih Dr.
Chem Univ Szeged 1941;1:17–26. Herzog at the University of Calgary. His
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Dr W. Herzog is a full Professor in Kinesiology

and Engineering with an adjunct appointment in
Medicine at the University of Calgary. He
received his BSc (equivalent) from the Federal
Technical Institute of Zurich, his PhD in Bio-
mechanics from the University of Iowa in 1985,
and completed a 2-year postdoctoral fellowship
in Biomechanics at the University of Calgary in
1987. His primary research interests in the area
of muscle mechanics include the theoretical
modelling of molecular events of force pro-
duction, skeletal muscle properties, and the con-
trol of synergistic muscles during cyclic movements.