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Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation
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Best R.B., Li B., Steward A., Daggett V., Clarke J. Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation. Biophys. J. 81:2001;2344-2356.
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Best, R.B.1
Li, B.2
Steward, A.3
Daggett, V.4
Clarke, J.5
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51
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0034616309
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Unfolding pathways of individual bacteriorhodopsins
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The first study of membrane protein unfolding. AFM and single-molecule force spectroscopy are combined to image and manipulate individual bacteriorhodopsin molecules. The force measurements show that the helices leave the membrane pairwise
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Oesterhelt F., Oesterhelt D., Pfeiffer M., Engel A., Gaub H.E., Muller D.J. Unfolding pathways of individual bacteriorhodopsins. Science. 288:2000;143-146 The first study of membrane protein unfolding. AFM and single-molecule force spectroscopy are combined to image and manipulate individual bacteriorhodopsin molecules. The force measurements show that the helices leave the membrane pairwise.
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(2000)
Science
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Oesterhelt, F.1
Oesterhelt, D.2
Pfeiffer, M.3
Engel, A.4
Gaub, H.E.5
Muller, D.J.6
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52
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0036932510
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Stability of bacteriorhodopsin alpha-helices and loops analyzed by single-molecule force spectroscopy
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Müller D.J., Kessler M., Oesterhelt F., Möller C., Oesterhelt D., Gaub H.E. Stability of bacteriorhodopsin alpha-helices and loops analyzed by single-molecule force spectroscopy. Biophys. J. 83:2002;3578-3588.
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Müller, D.J.1
Kessler, M.2
Oesterhelt, F.3
Möller, C.4
Oesterhelt, D.5
Gaub, H.E.6
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53
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0035957720
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Reversible unfolding of single RNA molecules by mechanical force
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Three different RNA sequences of increasing topological complexity were unfolded and refolded mechanically. The folding process occurs in equilibrium for the sequences that only contain secondary structure. However, in the presence of magnesium ions, which stabilize the tertiary structure, the unfolding of the P5abc domain from Tetrahymena thermophilia ribozyme occurs in nonequilibrium
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Liphardt J., Onoa B., Smith S.B., Tinoco I.J., Bustamante C. Reversible unfolding of single RNA molecules by mechanical force. Science. 292:2001;733-737 Three different RNA sequences of increasing topological complexity were unfolded and refolded mechanically. The folding process occurs in equilibrium for the sequences that only contain secondary structure. However, in the presence of magnesium ions, which stabilize the tertiary structure, the unfolding of the P5abc domain from Tetrahymena thermophilia ribozyme occurs in nonequilibrium.
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(2001)
Science
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Liphardt, J.1
Onoa, B.2
Smith, S.B.3
Tinoco, I.J.4
Bustamante, C.5
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54
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0037036070
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Equilibrium information from nonequilibrium measurements in an experimental test of Jarzynski's equality
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Single-molecule experiments with RNA were used to test Jarzynski's equality, which relates irreversible work to the equilibrium free energy difference
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Liphardt J., Dumont S., Smith S.B., Tinoco I. Jr., Bustamante C. Equilibrium information from nonequilibrium measurements in an experimental test of Jarzynski's equality. Science. 296:2002;1832-1835 Single-molecule experiments with RNA were used to test Jarzynski's equality, which relates irreversible work to the equilibrium free energy difference.
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(2002)
Science
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Liphardt, J.1
Dumont, S.2
Smith, S.B.3
Tinoco I., Jr.4
Bustamante, C.5
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55
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0344052669
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Molecular mechanistic origin of the toughness of natural adhesives fibres and composites
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Smith B.L., Schäffer T.E., Viani M., Thompson J.B., Frederick N.A., Kindt J., Belcher A., Stucky G.D., Morse D.E., Hansma P.K. Molecular mechanistic origin of the toughness of natural adhesives fibres and composites. Nature. 399:1999;761-763.
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Nature
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Smith, B.L.1
Schäffer, T.E.2
Viani, M.3
Thompson, J.B.4
Frederick, N.A.5
Kindt, J.6
Belcher, A.7
Stucky, G.D.8
Morse, D.E.9
Hansma, P.K.10
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56
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0035856905
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Bone indentation recovery time correlates with bond reforming time
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Thompson J.B., Kindt J.H., Drake B., Hansma H.G., Morse D.E., Hansma P.K. Bone indentation recovery time correlates with bond reforming time. Nature. 414:2001;773-776.
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(2001)
Nature
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Thompson, J.B.1
Kindt, J.H.2
Drake, B.3
Hansma, H.G.4
Morse, D.E.5
Hansma, P.K.6
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57
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0036977558
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The myosin coiled-coil is a truly elastic protein structure
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The first evidence of a protein structure that folds and refolds in thermodynamic equilibrium. The coiled coil of myosin II can produce forces of up to 25 pN during folding
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Schwaiger I., Sattler C., Hostetter D.R., Rief M. The myosin coiled-coil is a truly elastic protein structure. Nat. Materials. 1:2002;232-235 The first evidence of a protein structure that folds and refolds in thermodynamic equilibrium. The coiled coil of myosin II can produce forces of up to 25 pN during folding.
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(2002)
Nat. Materials
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, pp. 232-235
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Schwaiger, I.1
Sattler, C.2
Hostetter, D.R.3
Rief, M.4
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