Please use this identifier to cite or link to this item: http://hdl.handle.net/10995/111714
Title: Quantal Sarcomere-length Changes in Relaxed Single Myofibrils
Authors: Blyakhman, F.
Tourovskaya, A.
Pollack, G. H.
Issue Date: 2001
Publisher: Biophysical Society
Elsevier BV
Citation: Blyakhman F. Quantal Sarcomere-length Changes in Relaxed Single Myofibrils / F. Blyakhman, A. Tourovskaya, G. H. Pollack // Biophysical Journal. — 2001. — Vol. 81. — Iss. 2. — P. 1093-1100.
Abstract: We carried out experiments on single isolated myofibrils in which thin filaments had been functionally removed, leaving the connecting (titin) filaments as the sole agent taking up the length change. With technical advances that gave sub-nanometer detectability we examined the time course of single sarcomere-length change when the myofibril was ramp-released or ramp-stretched by a motor. The sarcomere-length change was stepwise. Step sizes followed a consistent pattern: the smallest was ∼2.3 nm, and others were integer multiples of that value. The ∼2.3-nm step quantum is the smallest consistent biomechanical event ever demonstrated. Although the length change must involve the connecting filament, the size of the quantum is an order of magnitude smaller than anticipated from folding of Ig- or fibronectin-like domains, implying either that folding occurs in sub-domain units or that other mechanisms are involved.
Keywords: CONNECTIN
FIBRONECTIN
ANIMAL CELL
ARTICLE
MUSCLE FIBRIL
NONHUMAN
PROTEIN DOMAIN
PROTEIN FOLDING
QUANTUM MECHANICS
RELAXATION TIME
SARCOMERE
SARCOMERE LENGTH
ANIMALIA
URI: http://hdl.handle.net/10995/111714
Access: info:eu-repo/semantics/openAccess
SCOPUS ID: 0034906672
ISSN: 0006-3495
Appears in Collections:Научные публикации, проиндексированные в SCOPUS и WoS CC

Files in This Item:
File Description SizeFormat 
2-s2.0-0034906672.pdf261,01 kBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.