Single Molecules
Single Molecules |
|
|
| 1 | List |
| 1 | Reversible unfolding of individual titin immunoglobulin domains by AFM M. Rief, (mrief@ph.tum.de )M. Gautel, F. Oesterhelt, (Filipp.oesterhelt@uniduesseldorf.de )JM. Fernandez, (jfernandez@columbia.edu )HE. Gaub, (gaub@lmu.de ) Science (1997-05-16) 276-5315 p.1109 Science publications Publisher : AMER ASSOC ADVANCEMENT SCIENCE, 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 USA. ISSN : 0036-8075 Abstract : Single-molecule atomic force microscopy (AFM) was used to investigate the 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. At large 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. Corresponding Author : Affiliation(s) : (0) LEHRSTUHL ANGEW PHYS,D-80799 MUNICH,GERMANY.; (1) EUROPEAN MOL BIOL LAB,BIOL STRUCT DIV,D-69012 HEIDELBERG,GERMANY.; (2) MAYO CLIN & MAYO FDN,DEPT PHYSIOL & BIOPHYS,ROCHESTER,MN 55905.; Key words : ATOMIC-FORCE MICROSCOPE; ELASTICITY; MUSCLE; PROTEINS; ADHESION; ENERGY; DNA Type : Article, English. 1997-05-16 Time cited 593; Journal impact factor for year 1997 equals 24.676 [0] BELL GI, 1978, SCIENCE, V200, P618 [1] BINNIG G, 1986, PHYS REV LETT, V56, P930 [2] BINNIG G, 1987, REV MOD PHYS, V59, P615 [3] BUSTAMANTE C, 1994, SCIENCE, V265, P1599 [4] CLUZEL P, 1996, SCIENCE, V271, P792 [5] DAMMER U, 1996, BIOPHYS J, V70, P2437 [6] ERICKSON HP, 1994, P NATL ACAD SCI USA, V91, P10114 [7] EVANS E, 1997, BIOPHYS J, V72, P1541 [8] FINER JT, 1994, NATURE, V368, P113 [9] FLORIN EL, 1994, SCIENCE, V264, P415 [10] FONG S, 1996, J MOL BIOL, V264, P624 [11] FRAUENFELDER H, 1991, SCIENCE, V254, P1598 [12] GAUTEL M, 1996, FEBS LETT, V385, P11 [13] GRUBMULLER H, 1996, SCIENCE, V271, P997 [14] HINTERDORFER P, 1996, P NATL ACAD SCI USA, V93, P3477 [15] LABEIT S, 1995, SCIENCE, V270, P293 [16] LEE GU, 1994, SCIENCE, V266, P771 [17] LINKE WA, 1996, J MOL BIOL, V261, P62 [18] MARKO JF, 1995, MACROMOLECULES, V28, P8759 [19] MARUYAMA K, 1977, J BIOCH, V82, P317 [20] MULLER DJ, 1995, J MOL BIOL, V249, P239 [21] PAN KM, 1994, BIOCHEMISTRY-US, V33, P8255 [22] PERKINS TT, 1995, SCIENCE, V268, P83 [23] POLITOU AS, 1994, FEBS LETT, V352, P27 [24] POLITOU AS, 1995, BIOPHYS J, V69, P2601 [25] POLITOU AS, 1996, J MOL BIOL, V255, P604 [26] RADMACHER M, 1994, SCIENCE, V265, P1577 [27] RIEF M, 1997, SCIENCE, V275, P1295 [28] SMITH SB, 1996, SCIENCE, V271, P795 [29] SOTERIOU A, 1993, P ROY SOC LOND B BIO, V254, P83 [30] WANG K, 1979, P NATL ACAD SCI USA, V76, P3698 |
|
Enter PubMed | Enter ISI Web of Science | 
|