Reverse engineering of the giant muscle protein titin

Hongbin Li, Wolfgang A. Linke, Andres Oberhauser, Mariano Carrion-Vazquez, Jason G. Kerkvliet, Hui Lu, Piotr E. Marszalek, Julio M. Fernandez

Research output: Contribution to journalArticle

370 Citations (Scopus)

Abstract

Through the study of single molecules it has become possible to explain the function of many of the complex molecular assemblies found in cells. The protein titin provides muscle with its passive elasticity. Each titin molecule extends over half a sarcomere, and its extensibility has been studied both in situ and at the level of single molecules. These studies suggested that titin is not a simple entropic spring but has a complex structure-dependent elasticity. Here we use protein engineering and single-molecule atomic force microscopy to examine the mechanical components that form the elastic region of human cardiac titin. We show that when these mechanical elements are combined, they explain the macroscopic behaviour of titin in intact muscle. Our studies show the functional reconstitution of a protein from the sum of its parts.

Original languageEnglish (US)
Pages (from-to)998-1002
Number of pages5
JournalNature
Volume418
Issue number6901
DOIs
StatePublished - Aug 29 2002
Externally publishedYes

Fingerprint

Connectin
Muscle Proteins
Elasticity
Protein Engineering
Muscles
Sarcomeres
Atomic Force Microscopy
Proteins

ASJC Scopus subject areas

  • General

Cite this

Li, H., Linke, W. A., Oberhauser, A., Carrion-Vazquez, M., Kerkvliet, J. G., Lu, H., ... Fernandez, J. M. (2002). Reverse engineering of the giant muscle protein titin. Nature, 418(6901), 998-1002. https://doi.org/10.1038/nature00938

Reverse engineering of the giant muscle protein titin. / Li, Hongbin; Linke, Wolfgang A.; Oberhauser, Andres; Carrion-Vazquez, Mariano; Kerkvliet, Jason G.; Lu, Hui; Marszalek, Piotr E.; Fernandez, Julio M.

In: Nature, Vol. 418, No. 6901, 29.08.2002, p. 998-1002.

Research output: Contribution to journalArticle

Li, H, Linke, WA, Oberhauser, A, Carrion-Vazquez, M, Kerkvliet, JG, Lu, H, Marszalek, PE & Fernandez, JM 2002, 'Reverse engineering of the giant muscle protein titin', Nature, vol. 418, no. 6901, pp. 998-1002. https://doi.org/10.1038/nature00938
Li H, Linke WA, Oberhauser A, Carrion-Vazquez M, Kerkvliet JG, Lu H et al. Reverse engineering of the giant muscle protein titin. Nature. 2002 Aug 29;418(6901):998-1002. https://doi.org/10.1038/nature00938
Li, Hongbin ; Linke, Wolfgang A. ; Oberhauser, Andres ; Carrion-Vazquez, Mariano ; Kerkvliet, Jason G. ; Lu, Hui ; Marszalek, Piotr E. ; Fernandez, Julio M. / Reverse engineering of the giant muscle protein titin. In: Nature. 2002 ; Vol. 418, No. 6901. pp. 998-1002.
@article{9deeff08676547a1962f910e8f5664d7,
title = "Reverse engineering of the giant muscle protein titin",
abstract = "Through the study of single molecules it has become possible to explain the function of many of the complex molecular assemblies found in cells. The protein titin provides muscle with its passive elasticity. Each titin molecule extends over half a sarcomere, and its extensibility has been studied both in situ and at the level of single molecules. These studies suggested that titin is not a simple entropic spring but has a complex structure-dependent elasticity. Here we use protein engineering and single-molecule atomic force microscopy to examine the mechanical components that form the elastic region of human cardiac titin. We show that when these mechanical elements are combined, they explain the macroscopic behaviour of titin in intact muscle. Our studies show the functional reconstitution of a protein from the sum of its parts.",
author = "Hongbin Li and Linke, {Wolfgang A.} and Andres Oberhauser and Mariano Carrion-Vazquez and Kerkvliet, {Jason G.} and Hui Lu and Marszalek, {Piotr E.} and Fernandez, {Julio M.}",
year = "2002",
month = "8",
day = "29",
doi = "10.1038/nature00938",
language = "English (US)",
volume = "418",
pages = "998--1002",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",
number = "6901",

}

TY - JOUR

T1 - Reverse engineering of the giant muscle protein titin

AU - Li, Hongbin

AU - Linke, Wolfgang A.

AU - Oberhauser, Andres

AU - Carrion-Vazquez, Mariano

AU - Kerkvliet, Jason G.

AU - Lu, Hui

AU - Marszalek, Piotr E.

AU - Fernandez, Julio M.

PY - 2002/8/29

Y1 - 2002/8/29

N2 - Through the study of single molecules it has become possible to explain the function of many of the complex molecular assemblies found in cells. The protein titin provides muscle with its passive elasticity. Each titin molecule extends over half a sarcomere, and its extensibility has been studied both in situ and at the level of single molecules. These studies suggested that titin is not a simple entropic spring but has a complex structure-dependent elasticity. Here we use protein engineering and single-molecule atomic force microscopy to examine the mechanical components that form the elastic region of human cardiac titin. We show that when these mechanical elements are combined, they explain the macroscopic behaviour of titin in intact muscle. Our studies show the functional reconstitution of a protein from the sum of its parts.

AB - Through the study of single molecules it has become possible to explain the function of many of the complex molecular assemblies found in cells. The protein titin provides muscle with its passive elasticity. Each titin molecule extends over half a sarcomere, and its extensibility has been studied both in situ and at the level of single molecules. These studies suggested that titin is not a simple entropic spring but has a complex structure-dependent elasticity. Here we use protein engineering and single-molecule atomic force microscopy to examine the mechanical components that form the elastic region of human cardiac titin. We show that when these mechanical elements are combined, they explain the macroscopic behaviour of titin in intact muscle. Our studies show the functional reconstitution of a protein from the sum of its parts.

UR - http://www.scopus.com/inward/record.url?scp=0037194788&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037194788&partnerID=8YFLogxK

U2 - 10.1038/nature00938

DO - 10.1038/nature00938

M3 - Article

VL - 418

SP - 998

EP - 1002

JO - Nature

JF - Nature

SN - 0028-0836

IS - 6901

ER -