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Titolo:
REVERSIBLE UNFOLDING OF INDIVIDUAL TITIN IMMUNOGLOBULIN DOMAINS BY AFM
Autore:
RIEF M; GAUTEL M; OESTERHELT F; FERNANDEZ JM; GAUB HE;
Indirizzi:
LEHRSTUHL ANGEW PHYS,AMALIENSTR 54 D-80799 MUNICH GERMANY LEHRSTUHL ANGEW PHYS D-80799 MUNICH GERMANY EUROPEAN MOL BIOL LAB,BIOL STRUCT DIV D-69012 HEIDELBERG GERMANY MAYO CLIN & MAYO FDN,DEPT PHYSIOL & BIOPHYS ROCHESTER MN 55905
Titolo Testata:
Science
fascicolo: 5315, volume: 276, anno: 1997,
pagine: 1109 - 1112
SICI:
0036-8075(1997)276:5315<1109:RUOITI>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
ATOMIC-FORCE MICROSCOPE; ELASTICITY; MUSCLE; PROTEINS; ADHESION; ENERGY; DNA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
31
Recensione:
Indirizzi per estratti:
Citazione:
M. Rief et al., "REVERSIBLE UNFOLDING OF INDIVIDUAL TITIN IMMUNOGLOBULIN DOMAINS BY AFM", Science, 276(5315), 1997, pp. 1109-1112

Abstract

Single-molecule atomic force microscopy (AFM) was used to investigatethe mechanical properties of titin, the giant sarcomeric protein of striated muscle. Individual titin molecules were repeatedly stretched, and the applied force was recorded as a function of the elongation. Atlarge extensions, the restoring force exhibited a sawtoothlike pattern, with a periodicity that varied between 25 and 28 nanometers. Measurements of recombinant titin immunoglobulin segments of two different lengths exhibited the same pattern and allowed attribution of the discontinuities to the unfolding of individual immunoglobutin domains. The forces required to unfold individual domains ranged from 150 to 300 piconewtons and depended on the pulling speed. Upon relaxation, refolding of immunoglobulin domains was observed.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 22:42:58