STEP SIZE IN ACTIVATED RABBIT SARCOMERES IS INDEPENDENT OF FILAMENT OVERLAP

2004 ◽  
Vol 04 (04) ◽  
pp. 485-498 ◽  
Author(s):  
EKATERINA M. NAGORNYAK ◽  
GERALD H. POLLACK ◽  
FELIX A. BLYAKHMAN

Investigations carried out on single cardiac and bumblebee myofibrils have shown stepwise sarcomere-length change of ~2.7 nm.1 We have carried out parallel measurements on single myofibrils from rabbit psoas muscle. Activated specimens were released or stretched using a motor-imposed ramp. With a high-resolution algorithm, we found that step sizes were always integer multiples of 2.7 nm, whether the length change was positive or negative, and independent of ramp velocity. Also, the influence of initial sarcomere length was studied, and found to be negligible. The value 2.7 nm, seen consistently, is equal to the linear repeat of actin monomers along the thin filament, a result that ties dynamical events to molecular structure, and places narrow constraints on any proposed molecular mechanism.

2002 ◽  
Vol 283 (3) ◽  
pp. C735-C742 ◽  
Author(s):  
Olga Yakovenko ◽  
Felix Blyakhman ◽  
Gerald H. Pollack

In attempting to deduce the size of the elementary molecular translation step, recent experiments using single myosin molecules translating over actin filaments have shown a consistent step size of 5.4 nm (10, 21). We have carried out parallel measurements on single myofibrils from rabbit cardiac muscle and bumblebee flight muscle. Activated specimens were released or stretched with a motor-imposed ramp, and the time course of length of individual sarcomeres was measured by projecting the image of the striations onto a linear photodiode array and tracking the spacing between A-band centroids. We confirmed the 5.4-nm step. With subnanometer precision, however, we find that this value is two times that of a more fundamental step size of 2.7 nm. Step sizes were always integer multiples of 2.7 nm, whether the length change was positive or negative. This value is equal to the linear repeat of actin monomers along the thin filament, a result that ties dynamic events to molecular structure and places narrow constraints on any proposed molecular mechanism.


2004 ◽  
Vol 25 (1) ◽  
pp. 37-43 ◽  
Author(s):  
Ekaterina Nagornyak ◽  
Felix Blyakhman ◽  
Gerald H. Pollack

1986 ◽  
Vol 17 (7) ◽  
pp. 19-29
Author(s):  
Isao Horiba ◽  
Shigenobu Yanaka ◽  
Akira Iwata ◽  
Nobuo Suzumura

Spine ◽  
2011 ◽  
Vol 36 (26) ◽  
pp. E1666-E1674 ◽  
Author(s):  
Gilad J. Regev ◽  
Choll W. Kim ◽  
Akihito Tomiya ◽  
Yu Po Lee ◽  
Hossein Ghofrani ◽  
...  

2016 ◽  
Vol 914 ◽  
pp. 35-46 ◽  
Author(s):  
Ying-Xu Zeng ◽  
Svein Are Mjøs ◽  
Fabrice P.A. David ◽  
Adrien W. Schmid

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