论文信息 - Stretching Single Protein Molecules: Titin Is a Weird Spring

Stretching Single Protein Molecules: Titin Is a Weird Spring

Titin is a huge protein with many immunoglobulin domains that provide elasticity to muscle. In his Perspective, Erickson discusses three analyses of single titan molecules--two on pp. [1109][1] and [1112][2] of this issue and one in this week's Nature . Molecular pulling on individual titin molecules with laser tweezers and atomic force microscopy reveals that it is an "entropic spring" that eventually loses its ability to recoil (renature) when large stretches of its immunoglobulin domains unravel. [1]: http://www.sciencemag.org/cgi/content/short/276/5315/1109 [2]: http://www.sciencemag.org/cgi/content/short/276/5315/1112

H. Erickson | H P Erickson

[1] W. Linke,et al. Towards a molecular understanding of the elasticity of titin. , 1996, Journal of molecular biology.

[2] H. Erickson,et al. Reversible unfolding of fibronectin type III and immunoglobulin domains provides the structural basis for stretch and elasticity of titin and fibronectin. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[3] S. Smith,et al. Folding-unfolding transitions in single titin molecules characterized with laser tweezers. , 1997, Science.

[4] Siegfried Labeit,et al. Titins: Giant Proteins in Charge of Muscle Ultrastructure and Elasticity , 1995, Science.

[5] R. M. Simmons,et al. Elasticity and unfolding of single molecules of the giant muscle protein titin , 1997, Nature.

[6] S. Martin,et al. Titin folding energy and elasticity , 1993, Proceedings of the Royal Society of London. Series B: Biological Sciences.

[7] H. Granzier,et al. Nonuniform elasticity of titin in cardiac myocytes: a study using immunoelectron microscopy and cellular mechanics. , 1996, Biophysical journal.

[8] M. Gautel,et al. A molecular map of titin/connectin elasticity reveals two different mechanisms acting in series , 1996, FEBS letters.