Nanomechanics of full-length nebulin: An elastic strain gauge in the skeletal muscle sarcomere

Vamsi K. Yadavalli, Jeffrey G. Forbes, Kuan Wang

研究成果: 雜誌貢獻文章同行評審

9 引文 斯高帕斯(Scopus)


Nebulin, a family of giant modular proteins (MW 700-800 kDa), acts as a F-actin thin filament ruler and calcium-linked regulator of actomyosin interaction. The nanomechanics of full length, native rabbit nebulin was investigated with an atomic force microscope by tethering, bracketing, and stretching full-length molecules via pairs of site-specific antibodies that were attached covalently, one to a protein resistant self-assembled monolayer of oligoethylene glycol and the other to the cantilever. Using this new nanomechanics platform that enables the identification of single molecule events via an unbiased analysis of detachment force and distance of all force curves, we showed that nebulin is elastic and extends to ∼1 μm by external force up to an antibody detachment force of ∼300-400 pN. Upon stretching, nebulin unravels and yields force spectra with craggy mountain range profiles with variable numbers and heights of force peaks. The peak spacings, analyzed by the model-independent, empirical Hilbert-Huang transform method, displayed underlying periodicities at ∼15 and ∼22 nm that may result from the unfolding of one or more nebulin modules between force peaks. Nebulin may act as an elastic strain gauge that interacts optimally with actin only under appropriate strain and stress. This stretch to match protein ruler may also exert a compressive force that stabilizes thin filaments against stress during contraction. We propose that the elasticity of nebulin is integral and essential in the muscle sarcomere. This article not subject to U.S. Copyright. Published 2009 by the American Chemical Society.

頁(從 - 到)7496-7505
出版狀態已發佈 - 七月 7 2009

ASJC Scopus subject areas

  • 材料科學(全部)
  • 凝聚態物理學
  • 表面和介面
  • 光譜
  • 電化學


深入研究「Nanomechanics of full-length nebulin: An elastic strain gauge in the skeletal muscle sarcomere」主題。共同形成了獨特的指紋。