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Titolo:
The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin measured by atomic force microscopy
Autore:
Rief, M; Gautel, M; Schemmel, A; Gaub, HE;
Indirizzi:
Univ Munich, Lehrstuhl Angew Phys, D-80799 Munich, Germany Univ Munich Munich Germany D-80799 l Angew Phys, D-80799 Munich, Germany European Mol Biol Lab, Biol Struct Div, D-69012 Heidelberg, Germany European Mol Biol Lab Heidelberg Germany D-69012 012 Heidelberg, Germany
Titolo Testata:
BIOPHYSICAL JOURNAL
fascicolo: 6, volume: 75, anno: 1998,
pagine: 3008 - 3014
SICI:
0006-3495(199812)75:6<3008:TMSOIA>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
ELASTIC PROTEIN; MOLECULAR MAP; EXPRESSION; TITIN/CONNECTIN; EXTENSION; TENASCIN; BINDING; CELLS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Rief, M Univ Munich, Lehrstuhl Angew Phys, Amalienstr 54, D-80799 Munich, Germany Univ Munich Amalienstr 54 Munich Germany D-80799 Munich, Germany
Citazione:
M. Rief et al., "The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin measured by atomic force microscopy", BIOPHYS J, 75(6), 1998, pp. 3008-3014

Abstract

The domains of the giant muscle protein titin (connectin) provide interaction sites for other sarcomeric proteins and fulfill mechanical functions. In this paper we compare the unfolding forces of defined regions of different titin isoforms by single-molecule force spectroscopy. Constructs comprising six to eight immunoglobulin (Ig) domains located in the mechanically active I-band part of titin are compared to those containing fibronectin III (Fn3) and lg domains from the A-band part. The high spatial resolution of the atomic force microscope allows us to detect differences in length as low as a few amino acids. Thus constructs of different lengths may be used as molecular rulers for structural comparisons with other modular proteins. Theunfolding forces range between 150 and 300 pN and differ systematically between the constructs. Fn3 domains in titin exhibit 20% lower unfolding forces than Ig domains. Fn3 domains from tenascin, however, unfold at forces only half those of titin Fn3 domains. This indicates that the tightly folded titin domains are designed to maintain their structural integrity, even under the influence of stretching forces. Hence, at physiological forces, unfolding is unlikely unless the forces are applied for a long time (longer than minutes).

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Documento generato il 03/12/20 alle ore 15:45:07